Results 71 to 80 of about 4,028 (99)
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Neutral endopeptidase and alcohol consumption, experiments in neutral endopeptidase-deficient mice
European Journal of Pharmacology, 2000Alcohol consumption was investigated in mice which were rendered deficient in the peptide-degrading enzyme neutral endopeptidase (EC 3.4.24.11) (NEP-/-) by gene targeting and compared to alcohol consumption in corresponding wild type mice (NEP+/+). Mice were offered a free choice to drink tap water or 10% alcohol. The NEP-/- mice consumed significantly
Kurt F. Hauser +8 more
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2004
Publisher Summary This chapter discusses the structural chemistry and the biological aspects of endopeptidase germination proteinase (GPR). The discovery that 10%–20% of the protein of dormant spores of Bacillus species is rapidly degraded during spore germination led to the identification of GPR as the endopeptidase that initiates this proteolysis ...
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Publisher Summary This chapter discusses the structural chemistry and the biological aspects of endopeptidase germination proteinase (GPR). The discovery that 10%–20% of the protein of dormant spores of Bacillus species is rapidly degraded during spore germination led to the identification of GPR as the endopeptidase that initiates this proteolysis ...
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An endopeptidase of bean leaves
Canadian Journal of Botany, 1970Bean leaves yielded an enzyme which hydrolyzed casein and hemoglobin to large peptide fragments. The protease exhibited maximal activity at pH 9 to 10, an isoelectric point of 8.8, and a molecular weight of about 100 000. During leaf growth the protease increased in a manner suggestive of a developmental role in the control of protein content.
Murray Foote, David Racusen
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An Introduction to the Endopeptidases
1992A very large number of proteolytic enzymes exist in the human body, and it is no easy matter to work out how they are involved in specific physiological and pathological processes. A concept that has proved helpful in this is that of splitting the enzymes into groups on the basis of (a) the type of reaction that they catalyse and (b) the chemical ...
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[42] Legumain: Asparaginyl endopeptidase
1994Publisher Summary This chapter describes asparaginyl endopeptidase from jack bean ( C. ensiformis ). During the characterization and purification of legumain from jack bean seeds, DNP-Pro-GIu-Ala-Asn-Val-Ile-Arg-NH 2 (DNP, dinitrophenyl) and DNP-Pro-GIu-Ala-Asn-NH 2 , which contain a sequence similar to that around one of the processing sites in ...
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Hydrolysis of N-formylmethionyl chemotactic peptides by endopeptidase 24.11 and endopeptidase 24.15
Peptides, 1996Endopeptidase 24.11 (EP 24.11), a membrane-bound cell surface enzyme, modulates chemotactic responsiveness of neutrophils to f-Met-Leu-Phe. It is unknown if the enzyme degrades potent formylmethionyl tetrapeptides or if an enzyme with similar activities, endopeptidase 24.15 (EP 24.15), degrades formylated chemotactic peptides.
Peter L. Almenoff +6 more
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2004
Publisher Summary This chapter presents an overview of the structural chemistry of PHEX (phosphate-regulating gene with homology to endopeptidase on the X chromosome). PHEX primary structure has been deduced from cDNA sequences cloned in several species including human. PHEX is a 749 amino acid protein.
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Publisher Summary This chapter presents an overview of the structural chemistry of PHEX (phosphate-regulating gene with homology to endopeptidase on the X chromosome). PHEX primary structure has been deduced from cDNA sequences cloned in several species including human. PHEX is a 749 amino acid protein.
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Proinsulin-Processing Endopeptidases
1994Knowledge of the gene structure of secreted proteins and analysis of their biosynthesis has revealed that many are initially produced as larger biologically inactive precursors that are subjected to limited proteolysis at sites marked by clusters of basic amino acids in characteristic linear sequences.
Deborah L. Bennett, John C. Hutton
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Inheritance of soybean endopeptidase
Biochemical Genetics, 1987Yun-Tzu Kiang, Joe-Yuan H. Doong
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