Download Identification of Genotypes of Blood Group A and B

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Identification
of Genotypes
of Blood
By Akira
The
human
blood
carbohydrate
groups
chains
galactosyltransferase
cell
surface.
to
both
but
determine
or BB
existence
of CRM
separating
CRM
but
T
certainty
not
governing
active
the
AO
by these
HE HUMAN
be determined
group
0
88
or
was
but
plasma.
88
should
transferase
responsible
cell
(B-enzyme)
for producing
surfaces,
with
in blood
A and
both
AA
or AO,
since
BB
or BO)
neither
activities
heterozygote.
anti-A-enzyme
B-enzymes
and
cally
inactive
that
but
protein
component
zygous
40
contains
A-
and
A,-
that
CRM
and
properties
genotypes,
certainty
by such
of the plasma.
indeed,
can
hetero-
Blood
Homozygous
parents.
A,A,
with
and
Heterozygous
pedigree.
of CRM
with
Assay
A persons
B substances
their
group
and
or 80
BB
nonallelic
was
inactive.
profiles
plasma.
plasma,
genotypes
and
for
the
demonstrated
blood
ABO
by
groups
heterozygous
model
of
In addition.
was
of the
red
family
A-enzyme
Immunoneutralization
AO
and
on the
examining
blood
common
of an enzymatically
in 0 plasma
any
and B-Enzyme
ofA-
The
transferase
ration
can
AO
locus.
be
and
The
80
genes
of the
nucleotide
from
natural
A-enzyme
M NaCI,
mM
NaN3,
acceptor.6
The
contained
2 mM
The
(‘H,
0.2%
assay,
bovine
and
reaction
ml).
The
25
was
reaction
mixture
was
also
reports
with
sugars,
and
less
than
subtracted
blood
Tris-CI,
group
the
pH
in the
that
and
enzyme
7.0,
was
N-acetylgalactosamine
was
UDP-galactose
was
New
England
98%
Nuclear
and
milk
as
with
Corp.
previously
Biogel
as determined
Purity
by its sugar
at
with
0.01
reported.5
Chemical
Co.
UDP-
purchased
was
from
composition.
was
prepared
further
from
purified
preparation
M
UDP-
previously
was
as
-60#{176}C.
(galactose-6-3H)
and
of the
purified
albumin.
Fucosyllactose
described,9
P-2.
enzymes)
form
I -3H)
UDP-galactose
from Amersham
purchased
human
(galactosamine-
enzyme
partially
diluted
as
control
as
mixture.
serum
Sigma
the
purified
reaction
were
from
hydrolysis
plasma
of partially
bovine
2
fucosyllactose
of
crude
synthesized
purchased
N-acetylgalactosamine
catalytic
in concentrated
1%
strip
(total
by a scintillation
minus
appropriately
containing
as
aliquot
withwater
radioactivity
complete
stored
used
37#{176}C.An
eluted
B-enzymes
and
used
to an arrow-shaped
of
case
of the
A-
reported,t8
use,
Before
3%
from
as a buffer.
and
case
I
the
was
mixture
The
For
0.5 MCi)
for spontaneous
in the
X-lOO,
was
16 hr at
and
reaction
Triton
enzyme.
6.5,
measured
a control.
10%
and
was
the
as
than
(less
eluate
UDPMnCI2,
(3H,
applied
(2 x 7 cm)
to correct
incubated
mixture
for
was
of the
nucleotide
pH
incubated
paper
6.5.
MI. for
15 mM
0.25%
pH
galactose
=
100
25 MM
ATP,
albumin,
imidazole,
mixture
In order
of the
UDP
mixture,
I mM
incorpoan analog
fucosyllactose,
buffer,
mM
radioactivity
counter.
serum
the
fucosyllactose,
reaction
MCi),
cacodylate
25 MM
donor,
0.5
by measuring
into
sugar
40 mM
B-enzyme
a sugar
sugar
assay
N-acetylgalactosamine
0.15
Activity
were assayed
activities
of sugar
The
METHODS
not
change
antiserum
plasma
group
during
against
previously.5
The
reconstituted
Vol. 55,
A-
and
(ACD
the
BO
of
A-enzyme
was
1 (January),
salted
pH
1980
at
was
out
7.0,
with
and
from
ofAB
were
by
was
activities
period
obtained
offspring
anticoagulant)
storage
purified
were
are
blood samples
were identified
B-transferase
in 0.01 M Tris-CI,
No.
samples
B who
genotypes
and
antibody
blood
A, and
A,O
whose
Fresh
blood
BB
phenotypes
individuals
The
Blood,
plasma.
AA
to
group
was
by gel
better
Sepharose
4B
than
(lot
no.
Samples
individuals
from
existence
filtration
AND
0
The
existence
Thus,
previously
approaches.
MATERIALS
B persons.
in homozygous
was
in addition
This article
be identified
A and
of heterozygous
source,
to the active
A- or B-enzyme,
while
homozygous
AA
and BB plasma
should
not contain
CRM.
Therefore,
it
should
be possible
to determine
genotypes
of blood
group
A and B persons
by examining
the immunobiochemical
that
the
without
of DEAE-cellulose
an enzymaticross-reactive
It is expected
plasma
impossible.
(20 MI) of the
the homozygote
it was found
that
0 plasma
contained
immunologically
BO
are
red
B persons,
both
been
in
those
the
group
group
neutralized
(CRM).5
and
blood
distinguish
Recently,
antibody
in blood
A and
nor
can
red
(A-
without
examingenotypes
(i.e.,
of phenotype
agglutinability
B-enzyme
from
the
absent
impossible,
to determine
A and
The
attached
in blood
allelic.
group
B persons
B substances
on
enzymes
0 persons.’
It has been
ing their family
pedigree,
not
known
to
residues
and
B
residues
producing
prepared.
is incompatible
be truly
for
It has
was
The
galactosyl-
persons
responsible
chromatography.
methods.
enzyme)
A
glycosyl
(A-enzyme)
demonstrated
affinity
of the
group
terminal
of group
from
plasma,
B) by
blood
groups
(ABO)
are
by the terminal
glycosyl
blood
80)
(CRM).
attached
to common
carbohydrate
chains
cell surface.
N-Acetylgalactosaminyltransferase
in
the
persons.
A-enzyme
80
and
and
AA
are
against
biochemical
expression
by
B persons
distinguished
and
(A
determined
or AO,
clearly
enzyme
group
AA
antibody
were
in homozygous
blood
group
protein
plasma
be
in blood
(i.e..
rabbit
in heterozygous
and
with
plasma
absent
and
to
A and
Yoshida
N-Acetylgalactosaminyltransferase
in blood
cross-reactive
AA
identified
known
surface.
genotypes
immunologically
homozygous
cell
enzymes
to homogeneity.
purified
are
red
(B-enzyme)
with
pedigree.
(ABO)
of the
Group
obtained
their
stored
2 mo.
as
at
Submitted
Address
-
Biochemical
E. Duarte
described
2 M (NH4)2S04
and
I 5#{176}C.
Department
of
Center,
in part
by
Biochemical
Duarte.
Genetics,
City
of
Hope
Calif
USPHS
Grant
HL-20301
and
NSF
Grant
FJ-5078.
did
Rabbit
the
Medical
60#{176}C.
plasma
prepared
stored
-
From
National
Supported
family
at
in the
least
x AB
©
1980
July
2. 1979;
reprint
requests
to
City
ofHope
Genetics,
Road,
Duarte,
by Grune
accepted
Calif
& Stratton,
September
Akira
21,
Yoshida.
National
Medical
1979.
Department
Center
of
/500
91010.
Inc.
0006-497I/80/550l0021$01.00/0
119
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120
AKIRA
Table
1 . Blo od Group
A- and B-Enzyme
Activity
Enzyme
in Plasma
YOSHIDA
100
Activity
90
Sample
Genotype
A
B
AA-1
AA-2
AA-3
A,A
17.2
A,A
9.2
A,A
17.1
AO-1
A,O
8.6
A,O
AO-2
Phenotype
-
7.2
A,
mean
(9 samples)
range
6.44,
t;
80
Q)
70
0
-
E
A
60
,
c:
w
2.8-16.8
A
Q)
BB-1
88
-
BB-2
BB
-
BO-1
80
-
BO-2
BO
-
Phenotype
15.3
range
composition
50
of the reaction
The enzyme
actosamine
activity
under
10) was
4B (1 mol
pl.
used
from
Sigma
was
prepared
gel)
assay.
of sugar
described
Co.
Plasma
and B-Enzyme
A-
A- and
AND
B-enzyme
described.’0
plasma
activities
plasma
nearly
were
in the
twice
that
homozygous
and
in Table
I.
I and AA-3
of heterozygous
plasma,
that
of the heterozygous
The A- and B-enzyme
and
B plasma
From the known
of the
differed
genotype
samples
were
higher
than
that
of
the B-enzyme
activity
(BB-2)
was similar
to
of phenotypes
widely
among
frequencies,
the
most,
A,
samples.
if not all,
to be heterozygous
A,O
The
plasma
Tris-CI,
pH
plasma
(or
albumin)
40
anti-A-enzyme
ofPlasma
A- and
Antibody
samples
7.0,
at
plasma
sl,
bated
at 4#{176}C
for
an assay
of the
immunoneutralization
A- and
B-enzyme
were more strongly
were
B-Enzyme
dialyzed
diluted
with
was mixed
with
antibody
(totaling
An
1%
various
50
0.01
of
M
aliquot
bovine
of
serum
amounts
of
sl) and
incu-
5 hr with shaking,
then subjected
remaining
transferase
activity.
profiles
indicated
that
activities
neutralized
50
d)
to an assay
with
homozygous
by the same
4
5
1%
bovine
and
of remaining
antibody.
the
6
7
8
9
10
ui
serum
AA-1
at
and
albumin
4’C
to
The
the
plasma
amount
of
for
A-enzyme
to
AA-3
plasma
result
5
hr.
activity.
in
AA
The
of
then
Prior
were
to
diluted
approximately
the
same activity
as that of AO-1 plasma.
The values represent
mean
values of duplicate
analysis
taking the control
(without
antibody)
as 100. (C) AA-1;
(A) AA-2;
(U)
AA-3;
(C) AO-1;
(M AO-2;
(t)
mixture
(1 :1 ) of AA-1 and 0 plasma.
antibody
than
those
and 0 plasma
heterozygous
of heterozygous
Existence
were
plasma.
plasma
has
Inactive
known
adsorbed
A-enzyme
uridine
that
with
Sepharose
4B
A,O
plasma,
and 0
Sepharose
4B column
plasma,
column
with
was
washed
(CRM)
but
not
A,-enzyme
Sepharose
can
be
5’-disphosphate.t
Utilizing
these adsorption
heterozygous
AO and BO
A,- and B-enzymes.
Aliquots
of homozygous
I
but
Protein
AO and BO Plasma
AA and BB Plasma
been
completely
(Figs.
profiles
of a
plasma
and 0
BB- I plasma
to that of corresponding
I and 2).
Cross-Reactive
in Heterozygous
in Homozygous
It
similar
(Figs.
of Enzymatically
be adsorbed
with
with
UDP-Sepharose
against
4#{176}C
overnight.
4
incubated
(totaling
adsorbed
containing
or BO.
Neutralization
by Anti-A-Enzyme
I
antibody
Immunologically
plasma.
activities
expected
3
I
and
2). The
immunoneutralization
mixture
(1:1)
of homozygous
AA-l
plasma
and a mixture
of homozygous
but the activity
of homozygous
AA-2
was only slightly
higher
than
that
of heterozygous
plasma.
Similarly,
the
B-enzyme
activity
of one
of the homozygous
plasma
(BB-l)
was distinctively
two heterozygous
samples,
but
of another
homozygous
plasma
2
I
of A-enzyme
in homozygous
by anti-A-enzyme
antibody.
mixed
with
various
amounts
with
samples
are presented
of homozygous
AA-
1
I
I
Fig. 1 . Immunoneutralization
and heterozygous
A0
plasma
dialyzed
plasma.
40
zl. was
mixing
RESULTS
Activities
activities
heterozygous
The enzyme
I
Antibody,
UDP-Sepharose
as previously
I
into
in the text.
Chemical
I
The
(N-acetylgal-
transferred
U
.
c:
1 7.5
subjected
EXPERIMENTS
A
Q)
10.6.
5.0-
enzyme
for B-enzyme)
conditions
U
20
in the text.
as percent
and galactose
obtained
for
was described
expressed
the assay
UDP/ml
was
mixture
was
A-enzyme
for
fucosyllactose
I 7C-Ol
plasma,
.
8.8
mean
of
0
30
10.0
B
aliquot
N
9.4
(7 samples)
An
U
40
eluted
4B,
with
B-enzyme
can
be
and
the
a
buffer
cannot
4B, but it can be adsorbed
(unpublished
observation).
properties,
CRM
present
in
plasma
was separated
from
(0.15
A,A,
plasma,
heterozygous
5 ml, were placed
on a
ml bed volume),
and the
I ml
of 0.1
M
cacodylate
buffer,
EDTA.
pH 7.0, containing
2 mM MnC12
and I mM
The eluate
was dialyzed
against
0.01 M Tris-
Cl,
7.0,
pH
containing
5% glycerol
and
I mM
EDTA,
From www.bloodjournal.org by guest on June 14, 2017. For personal use only.
GENOTYPE
IDENTIFICATION
OF ABO
121
SYSTEM
100
matography
>%
(final
go
:t
80
ci,
70
E
so that
60
Lu
The
I ml)
protein
was
used
4
N
30
.
0
inactivate
A
obtained
20
0)
not
A
10
:D
I
1
2
3
1
1
1
4
5
6
Antibody
,
ii
I.-.
I
I
7
8
neither
assay
of
adsorbed
respectively,
(NEP)
obtained
A- nor
B-enzyme
react
10
I
and
B-enzymes.
from
homozygous
A,A,
with
the
and
retained
B-enzymes
J___*
9
protein
had
A-
solution
I
nonenzyme
treatments
solution
for
to
by the
activi-
ty. When
the antibody
solution
was incubated
with
NEP
obtained
from
0, heterozygous
A,O,
and BO
plasma,
the treated
antibody
solution
lost its ability
to
t
0)
:s
the
above
50
.
above.
of about
CRM
activity.
The A- and B-enzymes
were completely
Sepharose
4B or to UDP-Sepharose
4B,
.4-
U
as described
volume
antibody,
its capacity
(Table
heterozygous
2).
A,O
BO
Fig. 2.
Immunoneutralization
of B-enzyme
in homozygous
BB
and heterozygous
80
plasma
by anti-A
enzyme
antibody.
The
dialyzed
plasma.
40 p1. was
mixed
with
various
amounts
of
antibody
(totaling
50 gil) and incubated
at 4’C for 5 hr. then
subjected
to an assay
of remaining
B-enzyme
activity.
Prior
to
mixing with antibody.
the BB-1 plasma was diluted with 1 % bovine
serum albumin
to result in approximately
the same activity
as that
of BO-1 plasma.
The values
represent
mean values
of duplicate
analysis
taking
the control
(without
antibody)
as 100. (C) BB-1 ; (A)
BB-2; (C) 80-1 ; () BO-2; (C) mixture
(1 :1) of BB-1 and 0 plasma.
contrast,
BB
the
for
These
and
ma, contained
CRM,
plasma
did not contain
In
and
NEP
plasma
treated
antibody
inactivating
results
did
A-
and
indicated
plasma,
as well
but homozygous
CRM.
that
as 0
A,A,
plas-
and
BB
DISCUSSION
It has been
known
that
the
groups
A and B subjects
cannot
agglutinability
enzyme
activities
Table
2.
of their
differ
Content
of CRM
blood.
widely
genotypes
be identified
Blood
among
in Homozygous
and in Heterozygous
blood
by the
group
A and B
individuals
with
and 88
A,A,
and 80
A,0
of
Plasma
Plasma
Percent
of Enzyme
Activity
Neutralized
by Antibody
and
placed
1.5
ml)
containing
EDTA.
on a CM-Sephadex
equilibrated
with
column
0.02
M
5% glycerol,
0.05
M
The column
was washed
equilibration
containing
buffer
and
0.08 M NaCI.
then
The
(bed
Tirs-CI,
NaCI,
with
Exp.
volume
pH
No.
7.0,
and
2 ml
I mM
of the
with 3 ml of the
protein
remaining
buffer
in the
column
was eluted
from the column
with 3 ml of the
buffer
containing
0.2 M NaC1
and precipitated
with
saturated
ammonium
sulfate.
The protein
(nonenzyme
protein,
NEP)
pH
7.0,
and
adjusted
then
To
was
the
to about
performed
I ml.
on the
separate
homozygous
were dialyzed
6.5, containing
dialyzed
volume
CRM
2
3
final
from
NEP
activity
assay
aliquots
of
BB and heterozygous
BO plasma,
5 ml,
against
0.025
M imidazole
buffer,
pH
15 mM MnCl2
and 0.15 M NaCI
at
4#{176}C
for 6 hr. The dialyzed
plasma
was
UDP-Sepharose
4B (bed
volume
3 ml)
with
the same
buffer,
and
the mixture
mixed
with
equilibrated
was
kept
buffer
Treated
with
NEP from
AA-1
84
78
Treated
with
NEP from
AO-1
<5
<5
with
buffer
with
NEP from
AA-2
80
Treated
with
NEP from
AO-2
<5
Treated
with
buffer
92
Treated
with
NEP from
<5
-
<5
-
Treated
with
NEP from
4
5
Treated
with
buffer
Treated
with
NEP
Treated
with
NEP from
from
72
95
BB-1
66
95
BO-1
<5
<5
Treated
with
buffer
-
88
Treated
with
NEP from
BB-2
-
92
Treated
with
NEP from
BO-2
-
NEP (nonenzyme
protein)
Tris-CI,
pH
7.0,
as control).
hr with
shaking.
An aliquot
further
analysis.
chro-
-
0 plasma
stirring
for 5 hr at 4#{176}C.
A small glass filter was used to
obtain
clear supernatant,
which
was then treated
with
saturated
ammonium
sulfate.
The protein
precipitate
was dialyzed
against
0.01 M Tris-CI,
ph 7.0, containing 5% glycerol
and I mM EDTA,
and subjected
to
column
-
phenotype
of antibody.
by CM-Sephadex
88
Treated
Treated
aliquot
fractionation
92
with
A, plasma
was
solution.
B-enzyme,
B-Enzyme
78
Treated
pooled
against
0.01 M Tris-CI,
of protein
solution
was
A CRM
A-Enzyme
Antibody
1
20
was
zI, was
prepared
mixed
with
and the mixture
of the mixture
as described
11
in the text.
An
40
MI of NEP (or 0.01
M
was
incubated
(or Tris buffer
at 4#{176}C
for 5
as control),
20
0, was mixed with 1 0 MI of partially
purified
A B-enzyme
and was
incubated
at 4#{176}C
for 5 hr with
shaking.
The incubated
enzyme
was
subjected
to an assay
described
in the
text.
of A- and B-enzyme
The
results
represent
activity
mean
under
values
the conditions
of duplicate
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122
AKIRA
Allelic
j
A
B
0
B
!gu1atory
Mde1
Non-Allelic
!‘txlel
Gene
Mde1
A
B
0
A
B
0
A
b
a
a
b
A
ct
A
6
A
B
B
B
B
Fig. 3.
Model for blood group
These
genes
are assumed
to
0
within
several
mosome
the
same
phenotypes,
and
types,
as reported
fore, the genotypes
their
blood
even
group
enzyme
of
the
same
nonallelic
A, and
geno-
heterozygous
and
of homozygous
different
from
BO
plasma.
A-
and
the
existence
of CRM
plasma,
but not
was unequivocally
ing CRM
A-enzyme)
and active
enzyme
and UDP-Sepharose
After
work
this
was
by
completed,
However,
tralization
of their
plasma,
by examining
the presence
or absence
plasma,
as described
in this article.
Although
the inheritance
of blood
answered.
In
the
past,
Furuhata
with
not
both
necessarily
ABO
chro-
of
Cis-AB
AB
x
0
is
postulated
originate
crossing-over
A and
by
to produce
B genes
a
is theoretically
assumes
that structural
are not allelic
and that
by allelic
According
to
this
produced
in 0 subjects,
shut
and
off
not
compatible
with
mendelian
inheritance,
and
genes
governing
the ABO blood groups
are generally
considered
to be allelic,
the
fundamental
question,
i.e.,
whether
or not ABO genes are truly allelic,
has not yet
been
of
regulatory
model,
since
silent.
The
only
in 0,
AA or BB plasma,
be concluded
that
blood
groups
are
truly
genes
for
expres-
both
a, 13, and
should
A and
not
be
B genes
demonstrated
heterozygous
either
It can
their
genes
CRM
are
existence
of
with the regulabe rejected.
should
be produced
AO
and
also
in homozygous
AA
and/or
present
results
indicate
that
CRM
in their
groups
discovery
offspring
CRM
in 0 plasma5
is incompatible
tory gene model,
so the model
can
In the nonallelic
model,
CRM
directly,
of CRM
does
is controlled
0.
homo-
more
in
possible
even between
true allelic
genes.
There
are three
conceivable
models
for ABO
locus
(ABO
cistron),
i.e.,
true
allelic
model,
nonallelic
model,
and regulatory
gene model
(Fig. 3). The regu-
sion
conclusion.
B subjects
can
immunoneu-
and
the
AB
In addition,
latory
gene
model
A- and B-enzymes
samples
of A,A2
plasma
that all these plasma
did
confirming
the above
of phenotype
A and
certainty
by examining
profiles
AO
AA and BB
by separat-
additional
pairs
two sites, one for A, or not
B.’2 Later,
the true allelic
by
an
Cis-AB
chromosome
Sepharose
4B (for
4B (for B-enzyme).
one
zygous
BB plasma
and four
were examined.
It was found
not contain
CRM,
The genotypes
be identified
with
in heterozygous
in homozygous
demonstrated
involving
B, or not
i.e.,
base
9.’
challenged
crossing-over.
heterozygous
AO and BO plasma
contain
CRM
in
addition
to the active
A- or B-enzyme,
while homozygous AA and BB plasma
do not contain
CRM.
In fact,
was
thousand
ABO locus.
be located
parents.’3”4
Komai
considered
that the Cis-AB
originated
from crossing-over
between
A and B genes
that
were pseudoallelic
but not allelic
in the strict
sense.’5
B-enzymes
were more strongly
neutralized
in homozygous
plasma
than
in heterozygous
plasma.
These
results
are
most
readily
interpreted
to mean
that
and BO
plasma,
model
for
expression,
profiles
distinctively
AO
one
model
activities.
The immunoneutralization
AA and BB plasma
were
those
with
by previous
iflvestigators.”
Therecannot
be identified
by measuring
YOSHIDA
BO
subjects,
but
BB subjects.
The
does not exist
in
refuting
the nonallelic
the genes governing
the
model.
ABO
allelic.
ACKNOWLEDGMENT
The
author
Professor
a
ALA,,
H.
AA2,
is indebted
to Professor
Taniguchi,
and
BB plasma
and
S. Miwa,
Professor
K.
Dr.
H. Yamaguchi,
Bender
for
providing
samples.
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1980 55: 119-123
Identification of genotype of blood group A and B
A Yoshida
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