... coagulating enzyme, plasmin, the starter bacteria, and the non-starter microflora are the main proteolytic agents involved in cheese ripening. Proteins are partially hydrolyzed by rennet and other native microbial enzymes to produce lower-molecular-weight compounds and are further broken down by pep ...
Ribosomes of Mouse Liver following
... from DMNA-treated mouse liver are normal as regards their activity in translating a synthetic messenger. Further more, the ribosomes that are membrane bound remain attached after disaggregation to monomers. Isolated poly somes were also found to be functionally normal following treatment, and the po ...
... from DMNA-treated mouse liver are normal as regards their activity in translating a synthetic messenger. Further more, the ribosomes that are membrane bound remain attached after disaggregation to monomers. Isolated poly somes were also found to be functionally normal following treatment, and the po ...
Specific Interaction of the PDZ Domain Protein PICK1 with the
... Protein kinase C (PKC)1 a belongs to a family of serine/ threonine protein kinases that are activated in response to a wide variety of hormones, mitogens, and neurotransmitters (1, 2). The PKC family is comprised of eleven isoforms, encoded by 10 genes. Individual cells typically express multiple is ...
... Protein kinase C (PKC)1 a belongs to a family of serine/ threonine protein kinases that are activated in response to a wide variety of hormones, mitogens, and neurotransmitters (1, 2). The PKC family is comprised of eleven isoforms, encoded by 10 genes. Individual cells typically express multiple is ...
Protein Similarity Score - Santa Clara Law Digital Commons
... See THOMAS E. CREIGHTON, PROTEINS: STRUCTURES AND MOLECULAR PRINCIPLES ...
... See THOMAS E. CREIGHTON, PROTEINS: STRUCTURES AND MOLECULAR PRINCIPLES ...
BEL β-trefoil: A novel lectin with antineoplastic properties in king
... Proteins of nonimmune origin that selectively bind and recognize carbohydrates without modifying them enzymatically are called lectins (Sharon 2007). In general, ligand binding precedes the fulfillment of an important biological function, which in some cases is still not known. Some members of this f ...
... Proteins of nonimmune origin that selectively bind and recognize carbohydrates without modifying them enzymatically are called lectins (Sharon 2007). In general, ligand binding precedes the fulfillment of an important biological function, which in some cases is still not known. Some members of this f ...
NF-kB as a primary regulator of the stress response
... large variety of cellular processes. The ubiquitin/ proteosome pathway mediates the regulated degradation of many proteins that play an essential role in cell cycle progression, immune response, transcriptional control, development and apoptosis. Activation of NF-kB is achieved through the signal-in ...
... large variety of cellular processes. The ubiquitin/ proteosome pathway mediates the regulated degradation of many proteins that play an essential role in cell cycle progression, immune response, transcriptional control, development and apoptosis. Activation of NF-kB is achieved through the signal-in ...
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... B. Living organisms acquire the energy they need for life processes through various metabolic pathways (primarily photosynthesis and cellular respiration). C. Chemical reactions in living things follow basic rules of chemistry and are usually regulated by enzymes. D. The unique chemical properties o ...
... B. Living organisms acquire the energy they need for life processes through various metabolic pathways (primarily photosynthesis and cellular respiration). C. Chemical reactions in living things follow basic rules of chemistry and are usually regulated by enzymes. D. The unique chemical properties o ...
Enzymes: The Biological Accelerators
... residue chain from the N-terminal of trypsinogen. This loss is accompanied by a change of conformation of the resultant protein to form the active form of the enzyme. Proenzymes allow the body to produce and control enzymes that could be harmful in the wrong place. E.g., trypsin catalyzes the breakd ...
... residue chain from the N-terminal of trypsinogen. This loss is accompanied by a change of conformation of the resultant protein to form the active form of the enzyme. Proenzymes allow the body to produce and control enzymes that could be harmful in the wrong place. E.g., trypsin catalyzes the breakd ...
Arginine-induced stimulation of protein synthesis and survival in
... to synthesize arginine (20, 37, 41), and the small intestine is a key site of net arginine synthesis in neonates (39, 42, 43). Thus the gut appears to play a critical role in maintaining arginine homeostasis in neonates (13, 40). Evidence from in vitro metabolic studies with primary cells and transf ...
... to synthesize arginine (20, 37, 41), and the small intestine is a key site of net arginine synthesis in neonates (39, 42, 43). Thus the gut appears to play a critical role in maintaining arginine homeostasis in neonates (13, 40). Evidence from in vitro metabolic studies with primary cells and transf ...
Lecture: 27 Fatty acid and triacyl glycerol biosynthesis Biosynthesis
... ii. Intermediates in fatty acid synthesis are covalently linked to the sulfhydryl group of an acyl carrier protein (ACP) whereas intermediates in fatty acid breakdown are bonded to coenzyme A. iii. The enzymes of fatty acid synthesis in animals are joined in a single polypeptide chain called fatty a ...
... ii. Intermediates in fatty acid synthesis are covalently linked to the sulfhydryl group of an acyl carrier protein (ACP) whereas intermediates in fatty acid breakdown are bonded to coenzyme A. iii. The enzymes of fatty acid synthesis in animals are joined in a single polypeptide chain called fatty a ...
Prokaryotic proteins of antioxidant defense in Trichomonas vaginalis
... resulting from two unpaired electrons in ground state of O2 molecule (triplet oxygen). It readily accepts electrons generated by normal oxidative metabolism of the cell. Processes causing uncoupling of electron transport can enhance the production of ROS, with mitochondria being a major source (23,8 ...
... resulting from two unpaired electrons in ground state of O2 molecule (triplet oxygen). It readily accepts electrons generated by normal oxidative metabolism of the cell. Processes causing uncoupling of electron transport can enhance the production of ROS, with mitochondria being a major source (23,8 ...
Lipid metabolism
... which makes a difficulty in their digestion by the water-soluble lipases. Emulsification means breaking of large fat globules into small ones that increase the surface area to interaction with lipases and increase the rate of digestion. The emulsification is done mainly by bile salts. Lipases in ...
... which makes a difficulty in their digestion by the water-soluble lipases. Emulsification means breaking of large fat globules into small ones that increase the surface area to interaction with lipases and increase the rate of digestion. The emulsification is done mainly by bile salts. Lipases in ...
A PEST-like Sequence in the N-Terminal Cytoplasmic Domain of
... and contain several potential phosphorylation sites (see Figure 1) (2). A PEST region spans residues 48-79 of the N-terminal cytoplasmic domain (2). Brondijk et al. (14) investigated the role of several of these sites located in the central cytoplasmic domain of Mal61p and found that serine295, loca ...
... and contain several potential phosphorylation sites (see Figure 1) (2). A PEST region spans residues 48-79 of the N-terminal cytoplasmic domain (2). Brondijk et al. (14) investigated the role of several of these sites located in the central cytoplasmic domain of Mal61p and found that serine295, loca ...
Chapter 2: Fuel Utilization and Muscle Metabolism During Exercise,
... lactic acid. As the glycogen levels drop in the red muscle fibers, they will rely more on fat. Since fat is less efficient than carbohydrate, intensity will decrease (pace will slow). At the other end of the spectrum, during mild exercise such as a brisk walk, muscles burn fat for fuel because the s ...
... lactic acid. As the glycogen levels drop in the red muscle fibers, they will rely more on fat. Since fat is less efficient than carbohydrate, intensity will decrease (pace will slow). At the other end of the spectrum, during mild exercise such as a brisk walk, muscles burn fat for fuel because the s ...
Human Skeletal Muscle Expresses a Glycogen
... were immediately frozen in liquid nitrogen. Liver biopsy samples were from control subjects or patients who had been previously studied for glycogen storage diseases, and the tissue was stored at ⫺80°C (37). Identification and sequence analysis of DNA encoding PP1 binding subunit GL. The National Ce ...
... were immediately frozen in liquid nitrogen. Liver biopsy samples were from control subjects or patients who had been previously studied for glycogen storage diseases, and the tissue was stored at ⫺80°C (37). Identification and sequence analysis of DNA encoding PP1 binding subunit GL. The National Ce ...
Dark Reactions
... chloroplast’s glyceraldehyde 3-phosphate dehydrogenase. Glyceraldehyde 3-phosphate dehydrogenase in the chloroplast is different than the cystolic glyceraldehyde 3-phosphate dehydrogenase. The chloroplast GAPDH is specific for NADPH rather than NADH. III. Regeneration of Ribulose 1,5-bisphosphate. T ...
... chloroplast’s glyceraldehyde 3-phosphate dehydrogenase. Glyceraldehyde 3-phosphate dehydrogenase in the chloroplast is different than the cystolic glyceraldehyde 3-phosphate dehydrogenase. The chloroplast GAPDH is specific for NADPH rather than NADH. III. Regeneration of Ribulose 1,5-bisphosphate. T ...
Full version (PDF file)
... proteins and nucleic acids are controlled by glyoxalase (Thornalley 1998). The glyoxalase system is present in the cytosol of all mammalian cells. It consists of two enzymes, glyoxalase I and glyoxalase II, and a catalytic amount of reduced glutathione (GSH). Physiologic α-oxoaldehydes, MG and glyox ...
... proteins and nucleic acids are controlled by glyoxalase (Thornalley 1998). The glyoxalase system is present in the cytosol of all mammalian cells. It consists of two enzymes, glyoxalase I and glyoxalase II, and a catalytic amount of reduced glutathione (GSH). Physiologic α-oxoaldehydes, MG and glyox ...
Functional analysis of a novel baculovirus envelope fusion protein
... applications. The research in this thesis focuses on the process of infection of baculoviruses, in particular the steps of virus attachment, entry and budding and the role of viral protein(s) involved there in. Published data about these processes available at the onset of this thesis will be presen ...
... applications. The research in this thesis focuses on the process of infection of baculoviruses, in particular the steps of virus attachment, entry and budding and the role of viral protein(s) involved there in. Published data about these processes available at the onset of this thesis will be presen ...
Bacterial production and the cycling of DOC
... DOC serves as the substrate for heterotrophic bacterial production in the ocean. Bacterial (net) production (BP) is measured through the uptake of tritiated substrates or from changes in bacterial cell numbers- large uncertainties (10x) in BP, BCD, GE. On average BP = 15-20% of PP, or about 10-15 GT ...
... DOC serves as the substrate for heterotrophic bacterial production in the ocean. Bacterial (net) production (BP) is measured through the uptake of tritiated substrates or from changes in bacterial cell numbers- large uncertainties (10x) in BP, BCD, GE. On average BP = 15-20% of PP, or about 10-15 GT ...
Enzymes - Weber State University
... Irreversible Inhibitors are toxic. In the laboratory they can be used to map the active site. These inhibitors often form covalent linkages to amino acids at the active site. DIPF (diisopropylphosphofluoridate) forms a covalent linkage to serine. If serine plays an important catalytic role for the e ...
... Irreversible Inhibitors are toxic. In the laboratory they can be used to map the active site. These inhibitors often form covalent linkages to amino acids at the active site. DIPF (diisopropylphosphofluoridate) forms a covalent linkage to serine. If serine plays an important catalytic role for the e ...
Enzymes
... Irreversible Inhibitors are toxic. In the laboratory they can be used to map the active site. These inhibitors often form covalent linkages to amino acids at the active site. DIPF (diisopropylphosphofluoridate) forms a covalent linkage to serine. If serine plays an important catalytic role for the e ...
... Irreversible Inhibitors are toxic. In the laboratory they can be used to map the active site. These inhibitors often form covalent linkages to amino acids at the active site. DIPF (diisopropylphosphofluoridate) forms a covalent linkage to serine. If serine plays an important catalytic role for the e ...
Lecture 6 - TCA cycle I - University of Lethbridge
... Catabolism of Proteins, Fats, and Carbohydrates The citric acid cycle is also called the Krebs cycle or the tricarboxylic acid (TCA) cycle. The citric acid cycle is the “hub” of the metabolic system. - Majority of carbohydrate, fatty acid and amino acid oxidation. - Majority of the generation of th ...
... Catabolism of Proteins, Fats, and Carbohydrates The citric acid cycle is also called the Krebs cycle or the tricarboxylic acid (TCA) cycle. The citric acid cycle is the “hub” of the metabolic system. - Majority of carbohydrate, fatty acid and amino acid oxidation. - Majority of the generation of th ...
Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.