Results 311 to 320 of about 82,787 (343)
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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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In silico methods to identify meat-derived prolyl endopeptidase inhibitors.
Food Chemistry, 2015T. Lafarga, P. O’Connor, M. Hayes
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Types and families of endopeptidases
Biochemical Society Transactions, 1991Alan J. Barrett, Neil D. Rawlings
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Purification and characterization of a prolyl endopeptidase isolated from Aspergillus oryzae
Journal of Industrial Microbiology & Biotechnology, 2013Chao Kang, Xiaowei Yu, Yan Xu
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