Download Full Text

Glycobiology vol. 11 no. 8 pp. 99R–105R, 2001
MINI REVIEW
The history of glycobiology in Japan
Akira Kobata
University of Tokyo and the Tokyo Metropolitan Institute of Gerontology,
5–18–2 Tsurumaki, Tama-shi, Tokyo 206–0034, Japan
Accepted on May 25, 2001
This mini review surveys the major accomplishments in the
field of glycoconjugates research in Japan, which were
made after World War II. It describes early movements in
the field of glycoconjugate research in Japan, development
of the new techniques to investigate structures of the sugar
chains of glycoconjugates, studies of the functions of the
sugar chain moieties, and the political movement in Japan to
support the basic research necessary for the development of
glycotechnology. As introduced in this short article, important
groundwork for glycobiology was made by Japanese
researchers.
Key words: glycobiology, N-linked sugar chain, O-linked
sugar chain, glycoprotein, proteoglycan, glycolipid
The early years after World War II
On August 15, 1945, World War II was over. Although great
chaos reigned across Japan for many years, natural science in
the country had slowly but steadily been recovering from
paralysis. In the field of carbohydrate research, major development started by the study of “homoglycans,” polysaccharides
consisting of only one type of sugar. Jiro Nikuni’s group at
Osaka University was actively investigating starch, and Choji
Araki and Susumu Hirase at Kyoto Technical University were
making progress in the study of galactans purified from agar,
which was a specialty of Japan.
The study of complex carbohydrates was not prosperous, but
some groups had already developed the seeds that would grow
into excellent programs. Among them, the strongest group was
built by Hajime Masamune at Tohoku University School of
Medicine. As a professor in the Department of Medical
Chemistry, he was examining pathological and biochemical
aspects of the glycoconjugates. He trained many excellent
students: Zensaku Yoshizawa, Noboru Hiyama, Keisuke
Tsurumi, and Sen-itiroh Hakomori. They were scattered as
leaders across several universities in the northeast of Japan and
built up the focus on glycoconjugate research.
In 1960, Tansuikabutsu Danwakai, a private workshop on
carbohydrate research, was organized by Tomoo Miwa (Tokyo
College of Education), Torao Ootsuki (Ochanomizu Women’s
University), and Susumu Murakami (Saitama University).
Although these three leaders were investigating plant
© 2001 Oxford University Press
carbohydrates and related enzymes, many young researchers
of animal glycoconjugates joined in this workshop.
By the end of 1960s, several other research cores for the
study of glycoconjugates were built in Japan. Tamio
Yamakawa (glycolipids), Ikuo Yamashina (glycoproteins),
Sakaru Suzuki and Kimiko Anno (proteoglycans), Toshiaki
Osawa (lectins), and Fujio Egami (glycosidases) were actively
developing their programs.
In 1976, the 8th International Carbohydrate Symposium,
chaired by Konoshin Onodera, professor at Kyoto University,
was held at Kyoto. This afforded a good chance to bring
together carbohydrate chemists and biochemists scattered in
Japan, and a desire to establish a new society for carbohydrate
research ran through the country. In 1978, an official workshop
of carbohydrate research (renamed as the Japanese Society of
Carbohydrate Research in 1987) was founded by the efforts of
Akira Misaki and others, and the first annual meeting was held
at Nakanoshima, Osaka. Yoshio Matsushima, professor at
Osaka University, was elected as the first president. It was
fortunate for carbohydrate researchers in Japan that from the
start the society included investigators interested in both
homoglycans and glycoconjugates.
Methods to analyze the structures of sugar chains
Interest in the sugar chains of glycoconjugates had been
stimulated in the early 1960s by elucidation of the antigenic
determinants of human blood types (Kabat, 1956; Watkins,
1966), and the molecular basis of antigenic conversion of
bacteria (Uchida and Robbins, 1963). This research area
attracted the interest of many biologists because the development of cell biology in the 1970s suggested that the sugar
chains of glycoconjugates might be working as signals in cell
to cell recognition.
Studies to develop sensitive and reliable methods to analyze
the structures of the sugar chains of glycoconjugates have been
actively performed in Japan. Methylation analysis reported by
Hakomori (1964)) was very useful, because complete methylation of heterosaccharides can be accomplished by a single
procedure. The problems of N-methylation of aminosugar
residues and the poor recovery of O-methylated N-methylaminosugars by gas chromatography were solved by the
successful synthesis of all partially O-methylated 2-N-methylglucosamines and by introduction of OV-17 as a liquid phase
(Tai et al., 1975).
Many eliminases (Yamagata et al., 1968; Hiyama and
Okada, 1975; Oike et al., 1982), exoglycosidases (Iijima and
Egami , 1971; Iijima et al., 1971; Kochibe, 1973; Uchida et al.,
99R
A. Kobata
1974; Arakawa-Ogata et al., 1977; Yoshima et al., 1979;
Ichishima et al., 1981; Amano and Kobata, 1986; Kitajima et
al., 1994), and endoglycosidases (Kitamikado and Ueno, 1970;
Koide and Muramatsu, 1974; Ito et al., 1975; Takasaki and
Kobata, 1976a,b; Endo and Kobata, 1976), were found as
useful tools for the studies of proteoglycans and glycoproteins.
These enzymes were isolated and their substrate specificities
were determined by Japanese investigators (Kitamikado and
Ueno, 1972; Nishigaki et al., 1974; Arakawa et al., 1974;
Fukuda and Matsumura, 1976; Takasaki and Kobata, 1976a,b;
Yamashita et al., 1976, 1980b, 1981b; Tai et al., 1977; Fukuda
et al., 1978; Mizuochi et al., 1984).
Development of hydrazinolysis (Takasaki et al., 1982),
radioisotope (Takasaki and Kobata, 1974), and fluorescent
taggings (Hase et al., 1986) of the oligosaccharides released by
either enzymatic or chemical means, fractionation of oligosaccharides by gel permeation (Yamashita et al., 1982a), highperformance liquid chromatography (Tomiya et al., 1988;
Higashi et al., 1990), and affinity chromatography with use of
immobilized lectin columns (Ogata et al., 1975) were also
developed. By elucidating the binding specificities of many
other immobilized lectins, serial lectin column chromatography was established as a very effective method to
fractionate and analyze the structures of N-linked sugar chains
(Kobata and Yamashita, 1993). Furthermore, application of the
frontal analysis (Kasai and Ishii, 1978) to lectin affinity
chromatography increased the value of this technique
(Okayama et al., 1985). Aminoglycopeptidase (Takahashi,
1977), which was introduced later, was also used as a very
effective tool.
Glycoproteins
Establishment of these reliable analytical methods enabled us
to study the structures of the N-linked sugar chains accurately.
Accumulation of structural data revealed the structural
diversity present in this major group of glycoprotein glycans.
Accordingly, finding of the occurrence of the hybrid-type
sugar chains (Tai et al., 1976), together with the structural
determination of the largest high mannose type sugar chain (Ito
et al., 1977), played important roles in the elucidation of an
unique biosynthetic pathway of the N-linked sugar chains by
Robbins et al. (1977) and Kornfeld’s group (Tabas et al.,
1978). Structural heterogeneity in the outer chain moieties of
the complex-type sugar chains, including occurrence of the
pentaantennary complex-type sugar chains (Yamashita et al.,
1982b), was also elucidated. The enzymatic bases for the
formation of these structures was revealed by the molecular
cloning of the glycosyltransferases (Schachter, 1995;
Nishikawa et al., 1992; Minowa et al., 1998).
Several novel sugar chains containing unique linkages have
been described by Japanese investigators. For example, Glc-Ser
was found in the blood coagulation factors (Hase et al., 1988).
Furthermore, the recent finding of a galactose cap on the
fucosyl residue linked to the trimannosyl core of the complextype N-linked sugar chains of octopus rhodopsin (Zhang et al.,
1997) indicates that this fucosyl residue should no longer be
considered as a termination signal as had long been believed.
100R
Glycolipids
Many glycolipids were found in animal tissues by Japanese
researchers (Hakomori, 1981). Structural studies of various
glycolipids found in fresh water animals by the group of Taro
Hori (Hori et al., 1983; Hori and Sugita, 1993), and those in
marine animals by Akira Hayashi’s group (Matsubara and
Hayashi, 1986) established novel insights into the diversity of
glycolipid structure. The number of glycolipids now known
has increased by the development of sensitive analytical
methods (Nagai and Iwamori, 1980). Finding of glycoceramidases (Ito and Yamagata, 1986) opened a new way to elucidate
the structures of the sugar chains of glycosphingolipids, and to
investigate their functional roles.
Success of the stereo-controlled α-sialylation of several
sugar residues by Kanie et al. (1988) opened a chemical way to
synthesize gangliosides in large scale (Prabhanjan et al., 1991;
Hasegawa and Kiso, 1994; Kiso and Hasegawa, 1994). This
greatly contributed to the progress of the glycobiology in the
field of glycolipids.
A human promyelocytic leukemic cell line, HL-60, is known
to have the dual potential to differentiate either to macrophages
by exposure to phorbol esters or to granulocytes by exposure to
dimethylsulfoxide. Masaki Saito and his collaborators (Saito,
1993) found that the amount of GM3 increases by differentiation
to macrophages, whereas the amount of neolacto-series
gangliosides increases by differentiation to granulocytes.
Interestingly, the addition of GM3 and neolacto-series gangliosides to the culture of HL-60 cells induced them to differentiate
into macrophages and granulocytes, respectively. These results
suggested that the glycolipids may play direct roles in the
differentiation of HL-60 cells.
Much evidence suggested that gangliosides may modulate
the mechanisms of growth hormone dependent transmembrane
signalling. The finding by Higashi and Yamagata (1992) and
Higashi et al. (1992) that GD1a and GD1b bind rather
specifically to the calmodulin in mouse brain, and modulate
calmodulin-dependent enzyme activation will open a promising
field for future investigation.
Sialic acids
A very unique series of researches in the field of sialic acid has
been reported by the group of Sadako Inoue and Yasuo Inoue.
Inoue and Iwasaki (1978) found an α2–8 linked polyNeuGc in
rainbow trout eggs. The importance of the polysialic acids in
the organization of neural tissues was later recognized by
many researchers after the finding of α2–8 linked polyNeuAc
in neural cell adhesion molecule. By investigating the
structures of polysialo-glycoproteins, purified from the cortical
granule of eggs of various fishes, Inoue and colleagues found
3-deoxy-D-glycero-D-galacto-nonulosonic
acid
(KDN)
(Nadano et al., 1986). KDN is an analogue of neuraminic acid,
in which the amino group is replaced by the hydroxyl group.
Further investigations revealed that KDN occurs linked to the
sugar chains of glycoproteins and glycolipids in the same
manner as sialic acids (Kanamori et al., 1990; Yu et al., 1991).
Recently, Japanese researchers have reported the occurrence of
KDN in mammalian tissues (Inoue et al., 1996). Therefore,
KDN is one of the new members of the family of sialic acids,
Glycobiology history in Japan
and its expression in relation to the development of multicellular organisms is a very important target for current study.
Proteoglycans
Although proteoglycans should also be considered as glycoproteins, in that their sugar chains (glycosaminoglycans) are
commonly linked to protein cores, the chains are much longer
(100–200 monosaccharide residues) than the regular N- and
O-linked sugar chains and contain many anionic residues, such
as uronic acids and O- and N-sulfated sugars. It had long been
believed that glycosaminoglycans have rather simple structures,
based on disaccharide repeats. However, development of the
reliable enzymatic methods to analyze the structures of the
glycosaminoglycan chains by Sakaru Suzuki’s group (Oike et al.,
1982) revealed the heterogeneity in these sugar chains. More
recently, Imanari and co-workers have developed a postcolumn derivatization method for analyzing the disaccharide
composition of glycosaminoglycans that can be applied to
tissue samples and microorganisms (Toyoda et al., 1996). In
addition, detailed structural studies of the linkage region have
revealed the presence of sulfate and phosphate on galactose
and xylose (Sugahara and Kitagawa, 2000).
Elucidation of the detailed structures of glycosaminoglycans
is also opening a new age for the study of proteoglycan
function in Japan. Some cell growth factors require binding to
heparan sulfate for the expression of their activities. Kimata
and colleagues found that basic fibroblast growth factor binds
specifically to a triple repeat of GlcNSO3-IdoA(2SO4) units
(Habuchi et al., 1992), and hepatocyte growth factor binds to
an octasaccharide region of heparan sulfate having at least two
GlcNSO3(6SO4)-IdoA(2SO4) units (Ashikari et al., 1995).
Purification and successful cloning of heparan sulfate 2-O
(Kobayashi et al., 1997) and 6-O-sulfotransferases (Habuchi
et al., 1998) led these investigators to propose that O-sulfations of
heparan sulfate are the key reactions for their cell growth
factor–related functions. Many examples indicating that the
sulfation of sugar chains is important in various cellular
recognition events in multi-cellular organisms were summarized
recently in Trends in Glycoscience & Glycotechnology
(Kawashima and Miyasaka, 2000; Takagaki and Ishido, 2000;
Habuchi, 2000; Sugahara and Yamada, 2000). Important roles
of aggrecan family proteoglycans in cell–cell and cell–substratum
interactions during the brain development have also been
reported by Oohira et al. (2000).
In addition, use of p-nitrophenyl-xyloside as a reagent to
inhibit specifically the chondroitin sulfate biosynthesis
(Okayama et al., 1973) revealed many important roles of the
glycosaminoglycans in the differentiation and developments of
multicellular organisms. These compounds have been in widespread use; based on this work new derivatives have been
made that can prime heparan sulfate (Fritz et al., 1994). The
use of xylosides has also stimulated other investigators to
examine other types of glycosides as primers (Sarkar et al.,
1995, 1997).
Turnover and degradation
Most glycoconjugates are degraded in lysosomes. Their
carbohydrate moieties are hydrolyzed by the concerted action
of glycosidases that reside in lysosomes. Because most of these
enzymes are exoglycosidases, the sugar chains are hydrolytically cleaved one by one from their nonreducing termini. In
such a degradation mechanism, the entire set of exoglycosidases necessary to cleave all monosaccharide units in a sugar
chain must be present for its complete degradation. If one of
the enzymes is missing, the catabolism of the sugar chain stops
at the point where the enzyme would have acted. Congenital
deficiencies are known in almost all of exoglycosidases. In
many of the deficiencies, glycolipids were shown to accumulate
in lysosomes of cells, giving rise to the lysosomal storage
diseases (Cervos-Navarro and Urich, 1995). Later on, the
discovery of oligosaccharides in the urine of patients with
lysosomal storage diseases (Wolfe et al., 1974), and their
structural study (Nishigaki et al., 1978; Yamashita et al., 1979,
1980a, 1981a; Ohkura et al., 1981) revealed that the N-linked
sugar chains of glycoproteins in the human body were released
by the action of an endo-β-N-acetylglucosaminidase, which
mainly occurs in the cytoplasm of cells (Tachibana et al., 1981).
Based on the finding that large amounts of Asn-oligosaccharides
are excreted in the urine of patients with fucosidosis (Yamashita
et al., 1979), who lack lysosomal α-fucosidase, it was confirmed
that the endo-β-N-acetylglucosaminidase does not work on the
N-linked sugar chains with fucosylated trimannosyl core:
Manα1–6(Manα1–3)Manβ1–4GlcNAcβ1–4(Fucα1–6)GlcNAc
(Tachibana et al., 1982). Structural studies of the oligosaccharides and Asn-oligosaccharides in the urine of lysosomal
storage diseases afforded much useful information regarding
the structures of the N-linked sugar chains of human glycoproteins. Recently, Seko et al. (1991) reported the occurrence
of peptide:N-glycanase, a similar enzyme as almond aminoglycopeptidase reported by Takahashi (1977), in animal tissues.
Because no oligosaccharide with the GlcNAcβ1–4GlcNAc group
at its reducing terminal was found in the urine samples of
patients with lysosomal storage diseases, the enzyme may not
work in the major catabolic pathway of glycoproteins, but
rather plays an important role in posttranslational modification
and/or remodification of glycoproteins.
Functional studies of glycoproteins
Turning to studies on the functional role of the N-linked sugar
chains, we must not forget the important discovery and
isolation of tunicamycin by Gakuzo Tamura and Akira Takatsuki
(Takatsuki et al., 1971). The compound is the structural
analogue of UDP-GlcNAc and contains a hydrophobic long
chain fatty acid. Because of this, it works as the inhibitor of
GlcNAc-1-phosphotransferase, that catalyzes the first step of the
biosynthetic pathway of dolichol oligosaccharide precursors.
Therefore, tunicamycin served as a specific inhibitor of the
N-linked sugar chain biosynthesis and was used as an essential
tool to elucidate many important roles of the sugar chains in
the differentiation and development of multicellular organisms
(Mizoguchi et al., 1981; Matsuda et al., 1982a,b).
Increase in the structural information of the sugar chains of
glycoconjugates has enabled researchers to consider their
functional roles at the molecular level. Examples include: (1)
The sugar chains of human chorionic gonadotropin that play an
essential role in the hormonal action of this glycohormone
(Kobata and Takeuchi, 1999). (2) Alteration of the sugar chain
101R
A. Kobata
structures of glycoproteins that occurs in various tumors
(Nishimura and Kobata, 1996; Yamashita and Kobata,
1996a,b; Kobata, 1996). Successful use of these alterations for
the diagnosis and prognosis of cancer has been reported in
Japan (Nishimura and Kobata, 1996; Yamashita and Kobata,
1996a). The idea that some of these alterations may be the
molecular basis of the unsocial behavior of malignant cells is
now becoming one of the important working hypotheses to
elucidate the mechanism of tumor metastasis. (3) Study of the
sugar chains of immunoglobulin G has revealed that the
galactose residues are playing an important role in the function
of the Fc portion of this humoral defense molecule (Tsuchiya
et al., 1989). Prominent deletion of galactose residue was
found to occur in the sugar chains of serum immunoglobulin G
obtained from patients with rheumatoid arthritis (Parekh et al.,
1985). These findings have activated a new movement to
elucidate the correlation of abnormalities of the sugar chains of
glycoproteins with diseases, and are opening a new research
area, which might be called glycopathology.
Genetic approaches
Development of gene technology in the past decade has been
accelerating the functional study of the sugar chains of glycoproteins. With use of this technology, we can now obtain
substantial amounts of bioactive proteins, which normally
occur in very small amounts. However, producing glycoproteins in bacteria often does not result in the expected
biological activities, because the sugar chains are not added.
This, in turn, has stimulated interest by molecular biologists in
the functional roles of the sugar chains.
To obtain recombinant glycoproteins, cultured animal cell
lines have been used instead of bacteria. However, through
comparative study of the sugar chains of γ-glutamyltranspeptidases purified from kidneys and livers of various mammals
(Kobata, 1992), occurrence of both organ and species differences
were found in the sugar chains of glycoproteins. In addition,
altered glycosylation occurs on recombinant glycoproteins
when expressed in tumor cell lines. Many of the cell lines used
have more or less malignant characters. Accordingly, structures of
the sugar chains of recombinant glycoproteins could be
affected by the cells used, despite having the same polypeptide
backbone. Comparative studies of the N-linked sugar chains of
natural human interferon-β1 (IFN-β1) and three recombinant
IFN-β1s produced by different mammalian cell lines, transfected with the gene coding for human IFN-β1, revealed that
their sugar patterns were different, although they all contain
the same number of complex-type sugar chains (Kagawa et al.,
1988). The differences occur both in the antennary structures
and in the structures of outer chain moieties. This situation
afforded a new way to elucidate the functions of the sugar
chains of glycoproteins, by comparatively investigating the
biological activities and the sugar chain structures of recombinant glycoproteins. A report by Takeuchi et al. (1989)) on
the comparative study of recombinant human erythropoietin
samples was the first example of such study. The examples
listed above indicate that investigation of the sugar chains is
essential for the sound development of gene technology and
protein engineering.
102R
Biotechnology and the future of glycosciences in Japan
Much information obtained from glycobiology research is expected
to be useful for the future development of biotechnology. In Japan,
a report on “The Policy for Promoting General R&D for Basic
Studies in Glycotechnology” was presented to the Minister of
State for Science and Technology on July 26, 1990, by the
Council for Aeronautics, Electronics and Other Advanced
Technologies. Based on this report, national projects on
glycotechnology sponsored by the Ministry of Science and
Technology, the Ministry of International Trade and Industry
(MITI), the Ministry of Health and Welfare (MHW), and the
Ministry of Agriculture, Forestry and Fisheries were started in
1991. The MHW project was mainly directed to drug delivery
systems, whereas the MITI project was directed at expanding
our understanding of the functions of the sugar chains of
glycoproteins and proteoglycans. A new genre in geneengineering opened with the production of mammalian cell
lines with transgenically modified sets of glycosyltransferases
(Fukuta et al., 2000), and the successful production of a
Saccharomyces cerevisiae mutant that can synthesize mammalian
N-glycans (Chiba et al., 1998). A new strategy for the synthesis
of oligosaccharides and glycopeptides using the reverse
reactions of exoglycosidases and endoglycosidases was developed by Ajisaka’s group (Matsuo et al., 1999; Ajisaka et al.,
1998). Successful cloning of N-acetylglucosaminyltransferase
IV (Minowa et al., 1998) and endo-β-N-acetylglucosaminidase
M, together with the finding of a recognition motif for
efficiently adding the O-linked sugar chains (Yoshida et al.,
1997) has provided new tools for glycotechnology. A new
analytical method for measuring binding of proteins to sugar
chains using a biosensor (Shinohara et al., 1997) was also a
major outcome of the MITI project.
Many prominent accomplishments were made in the past
decade supported by the grant money designated for glycobiology research based on the report described above. It had
been estimated that at least 12 different sialyltransferases exist
in mammals. Many of these enzymes were successfully cloned
and their properties were determined by Tsuji (1996). Cloning of
the glucuronyltransferase, which is responsible for the formation
of HNK-1 epitope: the SO4-3GlcAβ1–3Galβ1–4GlcNAc group,
and its transfection into COS-1 cells, revealed that the epitope
works as an important signal to induce neural cell morphogenesis (Terayama et al., 1997). L-selectin, which is expressed
on the surface of leukocytes, is considered to play an essential
role for the homing of peripheral lymphocytes. However, the
structure of its ligand remained unsolved for many years.
Uchimura et al. (1998) contributed to this field by identifying
sialyl-6-sulfo-Lex as the ligand of L-selectin.
The work cited in this mini review represents only a part of
the large number of glycobiology papers from Japan. Because
of space limitations, only some of the relevant papers have
been mentioned. Furthermore, glycobiology in Japan has both
benefited from and contributed to advances in glycobiology
around the globe. It is my hope that this mini review will help
readers in tracing the research activities of glycobiology in
Japan over the past half a century.
Glycobiology history in Japan
References
Ajisaka, K., Fujimoto, H., and Miyasato, M. (1998) An α-L-fucosidase from
Penicillium multicolor as a candidate enzyme for the synthesis of α-(1–3)-linked
fucosyl oligosaccharides by transglycosylation. Carbohydr. Res., 309,
125–129.
Amano, J., and Kobata, A. (1986) Purification and characterization of a novel
α-mannosidase from Aspergillus saitoi. J. Biochem., 99, 1645–1654.
Arakawa, M., Ogata, S., Muramatsu, T., and Kobata, A. (1974) β-galactosidases from jack bean meal and almond emulsin: Application for the
enzymatic distinction of Galβ1–4GlcNAc and Galβ1–3GlcNAc linkages.
J. Biochem., 75, 707–714.
Arakawa-Ogata, M., Muramatsu, T., and Kobata, A. (1977) α-L-fucosidases
from almond emulsin: Characterization of the two enzymes with different
specificities. Arch. Biochem. Biophys., 181, 353–358.
Ashikari, S., Habuchi, H., and Kimata, K. (1995) Characterization of heparan
sulfate oligosaccharides that bind to hepatocyte growth factor. J. Biol.
Chem., 270, 29586–29593.
Cervos-Navarro, J., and Urich, H. (1995) Disorders of lipid metabolism. In
Metabolic and Degenerative Diseases of the Central Nervous System,
Academic Press, San Diego, CA, pp. 221–395.
Chiba, Y., Suzuki, M., Yoshida, S., Yoshida, A., Ikenaga, H., Takeuchi, M.,
Jigami, Y., and Ichishima, E. (1998) Production of human compatible high
mannose-type (Man5GlcNAc2) sugar chains in Saccharomyces cerevisiae.
J. Biol. Chem., 273, 26298–26304.
Endo, Y., and Kobata, A. (1976) Partial purification and characterization of an
endo-α-N-acetylgalactosaminidase from the culture medium of Diplococcus
pneumoniae. J. Biochem., 80, 1–8.
Fritz, T., Lugemwa, F.N., Sarkar, A.K., and Esko, J.D. (1994) Biosynthesis of
heparan sulfate on β-D-xylosides depends on aglycone structure. J. Biol.
Chem. 269, 300–307.
Fukuda, M.N., and Matsumura, G. (1976) Endo-β-galactosidase from
Escherichia freundii: Purification and endoglycosidic action on keratan
sulfates, oligosaccharides, and blood group active glycoprotein. J. Biol.
Chem., 251, 6218–6225.
Fukuda, M.N., Watanabe, K., and Hakomori, S. (1978) Release of oligosaccharides from various glycosphingolipids by endo-β-galactosidase.
J. Biol. Chem., 253, 6814–6819.
Fukuta, K., Abe, R., Yokomatsu, T., Omae, F., Asanagi, M., and Makino, T.
(2000) Control of bisecting GlcNAc addition to N-linked sugar chains.
J. Biol. Chem., 275, 23456–23461.
Habuchi, H., Suzuki, S., Saito, T., Tamura, T., Harada, T., Yoshida, K., and
Kimata, K. (1992) Structure of a heparan sulfate oligosaccharide that binds
to basic fibroblast growth factor. Biochem. J., 285, 805–813.
Habuchi, H., Kobayashi, M., and Kimata, K. (1998) Molecular characterization
and expression of heparan-sulfate 6-sulfotransferase. J. Biol. Chem., 273,
9208–9213.
Habuchi, O. (2000) Sulfation of chondroitin sulfate and related sugar chains.
Trends Glycosci. Glycotech., 12, 307–319.
Hakomori, S. (1964) A rapid permethylation of glycolipid and polysaccharide
catalyzed by methylsulfinyl carbanion in dimethyl sulfoxide. J. Biochem.,
55, 205–208.
Hakomori, S. (1981) Glycosphingolipids in cellular interaction, differentiation,
and oncogenesis. Annu. Rev. Biochem., 50, 733–764.
Hase, S., Sugimoto, T., Takemoto, H., Ikenaka, T., and Schmid, K. (1986) The
structure of sugar chains of japanese quail ovomucoid. The occurrence of
oligosaccharides not expected from the classical biosynthetic pathway for
N-glycans; a method for the assessment of the structure of glycans present
in picomolar amounts. J. Biochem., 99, 1725–1733.
Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Suevoshi, T., Miyata, T.,
Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) A new
trisaccharide sugar chain linked to a serine residue in bovine blood coagulation
factors VII and IX. J. Biochem., 104, 867–868.
Hasegawa, A., and Kiso, M. (1994) Synthesis of sialyl Lewis X ganglioside
and analogs. Methods Enzymol., 242, 158–173.
Higashi, H., and Yamagata, T. (1992) Mechanism for ganglioside-mediated
modulation of a calmodulin-dependent enzyme. Modulation of calmodulindependent cyclic nucleotide phosphodiesterase activity through binding of
gangliosides to calmodulin and the enzyme. J. Biol. Chem., 267, 9839–9843.
Higashi, H., Ito, M., Fukaya, N., Yamagata, S., and Yamagata, T.(1990) Two
dimensional mapping by high-performance liquid chromatography of
oligosaccharides released from glycosphingolipids by endoglycoceramidase.
Anal. Biochem., 186, 355–362.
Higashi, H., Omori, A., and Yamagata, T. (1992) Calmodulin, a gangliosidebinding protein. Binding of gangliosides to calmodulin in the presence of
calcium. J. Biol. Chem., 267, 9831–9838.
Hiyama, K., and Okada, S. (1975) Crystallization and some properties of
chondroitinase from Arthrobacter aurescens. J. Biol. Chem., 250, 1824–1828.
Hori, T., and Sugita, M. (1993) Sphingolipids in lower animals. Prog. Lipid
Res., 32, 25–45.
Hori, T., Sugita, M., Ando, S., Tsukada, K., Shiota, K., Tsuzuki, M., and
Itasaka, O. (1983) Isolation and characterization of a 4-O-methylglucuronic acid-containing glycosphingolipid from spermatozoa of a fresh
water bivalve, Hyriopsis schlegelii. J. Biol. Chem., 258, 2239–2245.
Ichishima, E., Arai, M., Shigematsu, Y., Kumagai, H., and Sumida-Tanaka, R.
(1981) Purification of an acidic α-mannosidase from Aspergillus saitoi and
specific cleavage of 1, 2-α-mannosidic linkage in yeast mannan. Biochim.
Biophys. Acta, 658, 45–53.
Iijima, Y., and Egami, F. (1971) Purification of α-L-fucosidase from the liver
of a marine gastropod, Charonia lampas. J. Biochem., 70, 75–78.
Iijima, Y., Muramatsu, T., and Egami, F. (1971) Purification of α-L-fucosidase
from the liver of a marine gastropod, Turbo cornutus, and its action on
blood group substances. Arch. Biochem. Biophys., 145, 50–54.
Inoue, S., and Iwasaki, M. (1978) Isolation of a novel glycoprotein from the
eggs of rainbow trout: occurrence of disialosyl groups on all carbohydrate
chains. Biochem. Biophys. Res. Commun., 83, 1018–1023.
Inoue, S., Kitajima, K., and Inoue, Y. (1996) Identification of KDN (deaminoneuraminic acid) residues in mammalian tissues and human lung carcinoma
cells. Evidence of the occurrence of KDN-glycoconjugates in mammals.
J. Biol. Chem., 271, 24341–24344.
Ito, M., and Yamagata, T. (1986) A novel glycosphingolipid-degrading
enzyme cleaves the linkage between the oligosaccharide and ceramide of
neutral and acidic glycosphingolipids. J. Biol. Chem., 261, 14278–14282.
Ito, S., Muramatsu, T., and Kobata, A. (1975) Endo-β-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: Purification
and properties of the two enzymes with different specificities from
Clostridium perfringens. Arch. Biochem. Biophys., 171, 78–86.
Ito, S., Yamashita, K., Spiro, R.G., and Kobata, A. (1977) Structure of a carbohydrate moiety of a unit A glycopeptide of calf thyroglobulin. J. Biochem.,
81, 1621–1631.
Kabat, E.A. (1956) Blood Group Substances: Their Chemistry and Immunochemistry. Academic Press, New York.
Kagawa, Y., Takasaki, S., Utsumi, J., Hosoi, K., Shimizu, H., Kochibe, N., and
Kobata, A. (1988) Comparative study of the asparagine-linked sugar chains of
natural human interferon-β1 and recombinant human interferon-β1 produced by
three different mammalian cells. J. Biol. Chem., 263, 17508–17515.
Kanamori, A., Inoue, S., Iwasaki, M., Kitajima, K., Kawai, G., Yokoyama, S.,
and Inoue, Y. (1990) Deaminated neuraminic acid-rich glycoprotein of
rainbow trout egg vitelline envelope. Occurrence of a novel α2–8 linked
oligo(deaminated neuraminic acid) structure in O-linked glycan chains.
J. Biol. Chem., 265, 21811–21819.
Kanie, O., Kiso, M., and Hasegawa, A. (1988) Glycosylation using methylthioglycosides of N-acetylneuraminic acid and dimethyl(methylthio)sulfonium
triflate J. Carbohydr. Chem., 7, 501–506.
Kasai, K., and Ishii, S. (1978) Affinity chromatography of trypsin and related
enzymes. V. Basic studies of quantitative affinity chromatography. J. Biochem.,
84, 1051–1060.
Kawashima, H., and Miyasaka, M. (2000) Interaction of chondroitin sulfate
proteoglycans with selectins, CD44, and chemokines. Trends Glycosci.
Glycotech., 12, 283–294.
Kiso, M. and Hasegawa, A. (1994) Synthesis of ganglioside GM3 and analogs
containing modified sialic acids and ceramides. Methods Enzymol., 242,
173–183.
Kitajima, K., Kuroyanagi, H., Inoue, S., Ye, J., Troy, F.A. II, and Inoue, Y.
(1994) Discovery of a new type of sialidase, “KDNase”, which specifically
hydrolyzes deamino-neuraminyl (KDN) but not N-acylneuraminyl
linkages. J. Biol. Chem., 269, 21415–21419.
Kitamikado, M., and Ueno, R. (1970) Enzymatic degradation of whale
cartilage keratosulfate. III. Purification of a bacterial keratansulfatedegrading enzyme. Bull. Japan. Soc. Sci. Fish, 36, 1175–1180.
Kitamikado, M., and Ueno, R. (1972) Enzymatic degradation of whale
cartilage keratosulfate. IV. Properties of a bacterial keratansulfatedegrading enzyme. Bull. Japan. Soc. Sci. Fish, 38, 497–502.
Kobata, A. (1992) Structures and functions of the sugar chains of glycoproteins. Eur. J. Biochem., 209, 483–501.
Kobata, A. (1996) Cancer cells and metastasis: The Warren-Glick phenomenon: a molecular basis of tumorigenesis and metastasis. In Montreuil, J.,
103R
A. Kobata
Vliegenthart, J.F.G., and Schachter, H. (eds) Glycoproteins and Disease.
Elsevier, Amsterdam, Netherland, pp. 211–227.
Kobata, A., and Yamashita, K. (1993) Fractionation of oligosaccharides by
serial affinity chromatography with use of immobilized lectin columns. In
Fukuda, M, and Kobata, A. (eds) Glycobiology: A Practical Approach.
IRL Press, Oxford, UK, pp. 103–125.
Kobata, A., and Takeuchi, M. (1999) Structure, pathology, and function of the
N-linked sugar chains of human chorionic gonadotropin. Biochim.
Biophys. Acta, 1455, 315–326.
Kobayashi, M., Habuchi, H., Yoneda, M., Habuchi, O., and Kimata, K. (1997)
Molecular cloning and expression of chinese hamster ovary cell heparansulfate 2-sulfotransferase. J. Biol. Chem., 272, 13980–13985.
Kochibe, N. (1973) Purification and properties of α-L-fucosidase from
Bacillus fulminans. J. Biochem., 74, 1141–1149.
Koide, N., and Muramatsu, T. (1974) Endo-β-N-acetylglucosaminidase acting
on carbohydrate moieties of glycoproteins: Purification and properties of the
enzyme from Diplococcus pneumoniae. J. Biol. Chem., 249, 4897–4904.
Matsubara, T., and Hayashi, A. (1986) Structural studies on glycolipids of
shell fish. V. Gala-6 series glycosphingolipids of the marine snail,
Chlorostoma argyrostoma turbinatum. J. Biochem., 99, 1401–1408.
Matsuda, Y., Sakamoto, K., Mizuochi, T., Kobata, A., Tamura, G., and Tsubo, Y.
(1982a) Mating type specific inhibition of gametic differentiation of
Chlamydomonas reinhardtii by tunicamycin. Plant Cell Physiol., 22,
1607–1611.
Matsuda, Y., Sakamoto, K., Kikuchi, N., Mizuochi, T., Tsubo, Y., and Kobata, A.
(1982b) Two tunicamycin-sensitive components involved in agglutination
and fusion of Chlamydomonas reinhardtii gametes. Arch. Microbiol., 131,
87–90.
Matsuo, I., Isomura, M., and Ajisaka, K. (1999) Synthesis of an asparaginelinked core pentasaccharide by means of simultaneous inversion reactions.
J. Carbohyd. Chem., 18, 841–850.
Minowa, M.T, Oguri, S., Yoshida, A., Hara, T., Iwamatsu, A., Ikenaga, H., and
Takeuchi, M. (1998) cDNA cloning and expression of bovine UDP-Nacetylglucosamine: α-1, 3-mannoside β-1, 4-N-acetylglucosaminyltransferase IV. J. Biol. Chem., 273, 11556–11562.
Mizoguchi, A., Mizuochi, T., Kitazume, Y., Tamura, G., and Kobata, A.
(1981) Abnormal spicule formation induced by tunicamycin in early
development of sea urchin embryo. Cell Struct. Funct., 6, 341–346.
Mizuochi, T., Amano, J., and Kobata, A. (1984) New evidence of the substrate
specificity of endo-β-N-acetylglucosaminidase D. J. Biochem., 95, 1209–1213.
Nadano, D., Iwasaki, M., Endo, S., Kitajima, K., Inoue, S., and Inoue, Y.
(1986) A naturally occurring deaminated neuraminic acid, 3-deoxy-Dglycero-D-galacto-nonulosonic acid (KDN). Its unique occurrence at the
non-reducing ends of oligosialyl chains in polysialoglycoprotein of
rainbow trout eggs. J. Biol. Chem., 261, 11550–11557.
Nagai, Y., and Iwamori, M. (1980) A new approach to the analysis of ganglioside molecular species. In Svennerholm, L., Dreyfus, H., and Urban, P.-F.
(eds) Structure and Function of Gangliosides. Plenum, New York, NY, pp.
13–21.
Nishigaki, M., Muramatsu, T., Kobata, A., and Maeyama, K. (1974) The broad
aglycon specificity of α-L-fucosidase from marine gastropods. J. Biochem.,
75, 509–517.
Nishigaki, M., Yamashita, K., Matsuda, I., Arashima, S., and Kobata, A.
(1978) Urinary oligosaccharides of fucosidosis: Evidence of the
occurrence of X-antigenic determinant in serum-type sugar chains of
glycoproteins. J. Biochem., 84, 823–834.
Nishikawa, A., Ihara, Y., Hatakeyama, M., Kanagawa, K., and Taniguchi, N.
(1992) Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: bb-D-mannoside bb-1,4N-acetylglucosaminyltransferase III
from rat kidney.J. Biol. Chem., 267, 18199–18204.
Nishimura, R., and Kobata, A. (1996) Cancer cells and metastasis: Choriocarcinoma and hCG. In Montreuil, J., Vliegenthart, J.F.G., and Schachter, H.
(eds) Glycoproteins and Disease. Elsevier, Amsterdam, Netherlands,
pp. 185–195.
Ogata, S., Muramatsu, T., and Kobata, A. (1975) Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose.
J. Biochem., 78, 687–696.
Ohkura, T., Yamashita, K., and Kobata, A. (1981) Urinary oligosaccharides of
GM1-gangliosidosis: Structures of oligosaccharides excreted in the urine
of type 1 but not in the urine of type 2 patients. J. Biol. Chem., 256,
8485–8490.
Oike, Y., Kimata, K., Shinomura, T., Suzuki, S., Takahashi, N., and Tanabe, K.
(1982) A mapping technique for probing the structure of proteoglycan core
molecules. J. Biol. Chem., 257, 9751–9758.
104R
Okayama, M., Kimata, K., and Suzuki, S. (1973) The influence of p-nitrophenyl beta-d-xyloside on the synthesis of proteochondroitin sulfate by
slices of embryonic chick cartilage. J. Biochem., 74, 1069–1073.
Okayama, Y., Kasai, K., Nomoto, H., and Inoue, Y. (1985) Frontal affinity
chromatography of ovalbumin glycoasparagine on a concanavalin-A
Sepharose column. A quantitative study of the binding specificity of the
lectin. J. Biol. Chem., 260, 6882–6887.
Oohira, A., Matsui, F., Tokita, Y., Yamauchi, S., and Aono, S. (2000)
Molecular interactions of neural chondroitin sulfate proteoglycans in the
brain development. Arch. Biochem. Biophys., 374, 24–34.
Parekh, R.B., Dwek, R.A., Sutton, B.J., Fernandes, D.L., Leung, A.,
Stanworth, D., Rademacher, T.W., Mizuochi, T., Taniguchi, T.,
Matsuta, K., and others (1985) Association of rheumatoid arthritis and
primary osteoarthritis with changes in the glycosylation pattern of total
serum IgG. Nature, 316, 452–457.
Prabhanjan, H., Ishida, H., Kiso, M., and Hasegawa, A. (1991) Chemical
synthesis of gangliosides. Trends Glycosci. Glycotech., 3, 231–240.
Robbins, P.W., Hubbard, S.C., Turco, S.L., and Wirth, D.F. (1977) Proposal
for a common oligosaccharide intermediate in the synthesis of membrane
glycoproteins. Cell, 12, 893–900.
Saito, M. (1993) Bioactive gangliosides: differentiation inducers for
hematopoietic cells and their mechanism(s) of actions. Adv. Lipid Res., 25,
303–327.
Sarkar, A.K., Fritz, T.A., Taylor, W.H., and Esko, J.D. (1995) Disaccharide
uptake and priming in animal cells: Inhibition of sialyl Lewis X by
acetylated Galβ1, 4GlcNAcαO-naphthalenemethanol. Proc. Natl Acad.
Sci. USA, 92, 3323–3327.
Sarkar, A.K., Rostand, K.S., Jain, R.K., Matta, K.L., and Esko, J.D. (1997)
Fucosylation of disaccharide precursors of sialyl LewisX inhibit selectinmediated cell adhesion. J. Biol. Chem. 272, 25608–25616.
Seko, A., Kitajima, K., Inoue, S., and Inoue, Y. (1991) Peptide:N-glycosidase
activity found in the early embryo of Oryzias latipes (medaka fish). The
first demonstration of the occurrence of peptide:N-glycosidase in animal
cells and its implication for the presence of a de-N-glycosylation system in
living organisms. J. Biol. Chem., 266, 22110–22114.
Schachter, H. (1995) Glycosyltransferases involved in the synthesis of N-glycan
antennae. In Montreuil, J., Vliegenthart, J.F.G., and Schachter, H. (eds)
Glycoproteins. Elsevier, Amsterdam, Netherlands, pp. 153–199.
Shinohara, Y., Sota, H., and Hasegawa, Y. (1997) Novel approach for the
analysis of interaction between sugar chains and carbohydrate-recognizing
molecules using a biosensor based on surface plasmon resonance. In
Townsend, R.R. (ed) Techniques in Glycobiology. Marcel Dekker, New
York., pp. 209–228.
Sugahara, K., and Kitagawa, H. (2000) Recent advances in the study of the
biosynthesis and functions of sulfated glycosaminoglycans. Curr. Opin.
Struct. Biol., 10, 518–527.
Sugahara, K., and Yamada, S. (2000) Structure and function of oversulfated
chondroitin sulfate variants: Unique sulfation patterns and neuroregulatory
activities. Trends Glycosci. Glycotech., 12, 321–349.
Tabas, I., Schlesinger, S., and Kornfeld, S. (1978) Processing of high mannose
oligosaccharides to form complex type oligosaccharides on the newly
synthesized polypeptides of the vesicular stomatitis virus G protein and the
IgG heavy chain. J. Biol. Chem., 253, 716–722.
Tachibana, Y., Yamashita, K., Kawaguchi, M., Arashima, S., and Kobata, A.
(1981) Digestion of asparagine-linked oligosaccharides by endo-β-Nacetylglucosaminidase in the human skin fibroblasts obtained from fucosidosis patients. J. Biochem., 90, 1291–1296.
Tachibana, Y., Yamashita, K., and Kobata, A. (1982) Substrate specificity of
mammalian endo-β-N-acetylglucosaminidase: Study with the enzyme of rat
liver. Arch. Biochem. Biophys., 214, 199–210.
Tai, T., Yamashita, K., and Kobata, A. (1975) Synthesis and mass-fragmentographic analysis of partially O-methylated 2-N-methylglucosamines.
J. Biochem., 78, 679–686.
Tai, T., Yamashita, K., Ito, S., and Kobata, A. (1976) Structures of the
carbohydrate moiety of ovalbumin glycopeptide III and the difference in
specificity of endo-β-N-acetylglucosaminidases CII and H. J. Biol. Chem.,
252, 6687–6694.
Tai, T., Yamashita, K., and Kobata, A. (1977) The substrate specificities of
endo-β-N-acetylglucosaminidases CII and H. Biochem. Biophys. Res.
Commun., 78, 434–441.
Takagaki, K., and Ishido, K. (2000) Synthesis of chondroitin sulfate oligosaccharides using enzymatic reconstruction. Trends Glycosci. Glycotech.,
12, 295–306.
Glycobiology history in Japan
Takahashi, N. (1977) Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun., 76, 1194–1201.
Takasaki, S., and Kobata, A. (1974) Microdetermination of individual neutral
and amino sugars and N-acetylneuraminic acid in complex saccharides.
J. Biochem., 76, 783–789.
Takasaki, S., and Kobata, A. (1976a) Purification and characterization of an
endo-β-galactosidase produced by Diplococcus pneumoniae. J. Biol.
Chem., 251, 3603–3609.
Takasaki, S., and Kobata, A. (1976b) Chemical characterization and distribution
of ABO blood group active glycoprotein in human erythrocyte membrane.
J. Biol. Chem., 251, 3610–3615.
Takasaki, S., Mizuochi, T., and Kobata, A. (1982) Hydrazinolysis of asparaginelinked sugar chains to produce free oligosaccharides. Methods Enzymol.,
83, 263–268.
Takatsuki, A., Arima, K., and Tamura, G. (1971) Tunicamycin, a new antibiotic I.
Isolation and characterization of tunicamycin. J. Antibiot., 24, 215–223.
Takeuchi, M., Inoue, N., Strickland, T.W., Kubota, M., Wada, M.,
Shimizu, R., Hoshi, S., Kozutsumi, H., Takasaki, S., and Kobata, A. (1989)
Relationship between sugar chain structure and biological activity of
recombinant human erythropoietin produced in Chinese hamster ovary
cells. Proc. Natl Acad. Sci. USA, 86, 7819–7822.
Terayama, K., Oka, S., Seiki, T., Miki, Y., Nakamura, A., Kozutsumi, Y.,
Takio, K., and Kawasaki, T. (1997) Cloning and functional expression of a
novel glucuronyltransferase involved in the biosynthesis of the carbohydrate epitope HNK-I. Proc. Natl Acad. Sci. USA, 94, 6093–6098.
Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y., and Takahashi, N.
(1988) Analysis of N-linked oligosaccharides using a two-dimentional
mapping technique. Anal. Biochem., 171, 73–90.
Toyoda, H., Nagashima, T., Hirata, R., Toida, T., and Imanari T. (1996)
Sensitive high-performance liquid chromatographic method with fluorometric
detection for the determination of heparin and heparan sulfate in biological
samples: application to human urinary heparan sulfate. J. Chromatogr Biomed.
Sci. Appl., 704, 19–24.
Tsuchiya, N., Endo, T., Matsuta, K., Yoshinoya, S., Aikawa, T., Kosuge, E.,
Takeuchi, F., Miyamoto, T., and Kobata, A. (1989) Effects of galactose
depletion from oligosaccharide chains on immunological activities of
human IgG. J. Rheumatol., 16, 285–290.
Tsuji, S. (1996) Molecular cloning and functional analysis of sialyltransferases.
J. Biochem., 120, 1–13.
Uchida, T., and Robbins, P.W. (1963) Analysis of serologic determinant
groups of the Salmonella E-group O-antigen. Biochemistry, 2, 663–668.
Uchida, Y., Tsukada, Y., and Sugimori, T. (1974) Production of microbial
neuraminidases induced by colominic acid. Biochim. Biophys. Acta, 350,
425–431.
Uchimura, K., Muramatsu, H., Kadomatsu, K., Fan, Q.W., Kurosawa, N.,
Mitsuoka, C., Kannagi, R., Habuchi, O., and Muramatsu, T. (1998)
Molecular cloning and characterization of an N-acetylglucosamine-6-Osulfotransferase. J. Biol. Chem., 273, 22577–22583.
Watkins, W.M. (1966) Blood group specific substances. In Gottschalk, A. (ed)
Glycoproteins. Elsevier, Amsterdam, Netherlands, pp. 462–515.
Wolfe, L.S., Senior, R.G., and Ng Ying Kin, N.M.K. (1974) The structures of
oligosaccharides accumulating in the liver of GM1-gangliosidosis Type I.
J. Biol. Chem., 249, 1828–1838.
Yamagata, T., Saito, H., Habuchi, O., and Suzuki, S. (1968) Purification and
properties of bacterial chondroitinases and chondrosulfatases. J. Biol.
Chem., 243, 1523–1535.
Yamashita, K., and Kobata, A. (1996a) Cancer cells and metastasis: Hepatocellular carcinoma. In Montreuil, J., Vliegenthart, J.F.G., and Schachter, H.
(eds) Glycoproteins and Disease. Elsevier, Amsterdam, Netherlands,
pp. 197–210.
Yamashita, K., and Kobata, A. (1996b) Carcinoembryonic antigen and related
normal antigens. In Montreuil, J., Vliegenthart, J.F.G., and Schachter, H.
(eds) Glycoproteins and Disease. Elsevier, Amsterdam, Netherlands,
pp. 229–239.
Yamashita, K., Tachibana, Y., Takasaki, S., and Kobata, A. (1976) ABO blood
group determinants with branched cores. Nature, 262, 703–704.
Yamashita, K., Tachibana, Y., Takada, S., Matsuda, I., Arashima, S., and
Kobata, A. (1979) Urinary glycopeptides of fucosidosis. J. Biol. Chem.,
254, 4820–4827.
Yamashita, K., Tachibana, Y., Mihara, K., Okada, S., Yabuuchi, H., and
Kobata, A. (1980a) Urinary oligosaccharides of mannosidosis. J. Biol.
Chem., 255, 5126–5133.
Yamashita, K., Ichishima, E., Arai, M., and Kotata, A. (1980b) An α-mannosidase purified from Aspergillus saitoi is specific for α1, 2 linkages.
Biochem. Biophys. Res. Commun., 96, 1335–1342.
Yamashita, K., Ohkura, T., Okada, S., Yabuuchi, H., and Kobata, A. (1981a)
Urinary oligosaccharides of GM1-gangliosidosis: Different excretion
patterns of oligosaccharides in the urine of type 1 and type 2 subgroups.
J. Biol. Chem., 256, 4789–4798.
Yamashita, K., Ohkura, T., Yoshima, H., and Kobata, A. (1981b) Substrate
specificity of diplococcal β-N-acetylhexosaminidase, a useful enzyme for
the structural studies of the complex type asparagine-linked sugar chains.
Biochem. Biophys. Res. Commun., 100, 226–232.
Yamashita, K., Mizuochi, T., and Kobata, A. (1982a) Analysis of oligosaccharides
by gel filtration. Methods Enzymol., 83, 105–126.
Yamashita, K., Kamerling, J.P., and Kobata, A. (1982b) Structural study of the
carbohydrate moiety of hen ovomucoid: Occurrence of a series of pentaantennary complex-type asparagine-linked sugar chains. J. Biol. Chem.,
257, 12809–12814.
Yoshida, A., Suzuki, M., Ikenaga, H., and Takeuchi, M. (1997) Discovery of
the shortest sequence motif for high level mucin-type O-glycosylation.
J. Biol. Chem., 272, 16884–16888.
Yoshima, H., Takasaki, S., Ito-Mega, S., and Kobata, A. (1979) Purification of
Almond emulsin α-L-fucosidase I by affinity chromatography. Arch. Biochem.
Biophys., 194, 394–398.
Yu, S., Kitajima, K., Inoue, S., and Inoue, Y. (1991) Isolation and structural
elucidation of novel type of ganglioside, deaminated neuraminic acid
(KDN)-containing glycosphingolipid, from rainbow trout sperm. The first
example of the natural occurrence of KDN-ganglioside, (KDN)GM3.
J. Biol. Chem., 266, 21929–21935.
Zhang, Y., Iwasa, T., Tsuda, M., Kobata, A., and Takasaki, S. (1997) A novel
monoantennary complex-type sugar chain found in octopus rhodopsin:
occurrence of the Galβ1→4Fuc group linked to the proximal N-acetylglucosamine residue of the trimannosyl core. Glycobiology, 7, 1153–1158.
105R