[Proteolysis of simple glyprolines by leucine aminopeptidase and enzymes from nasal slime, brain membranes, and rat blood]

Autor:	K V, Shevchenko, T V, V'iunova, I Iu, Nagaev, L A, Andreeva, N F, Miasoedov
Rok vydání:	2014
Předmět:	Leucyl Aminopeptidase Proline Proteolysis Glycine Animals Brain Peptides Enzymes Rats
Zdroj:	Bioorganicheskaia khimiia. 39(3)
ISSN:	0132-3423
Popis:	Proteolysis of Pro-Gly-Pro-Leu, Pro-Gly-Pro-Gly and Pro-Gly-Pro were studied comparatively to Met-Glu-His-Phe-Pro-Gly-Pro (semax). It is shown that all three peptides are considerably more stable to proteolysis by N-leucine-aminopeptidase (EC 3.4.11.1, Sigma, type VI, 9.2 units/mg), and by enzymes of nasal slime, brain microsomal fractions, and rat blood. Metabolites of the proteolysis showed that semax derives His-Phe-Pro-Gly-Pro only, Pro-Gly-Pro-Leu forms Gly-Pro-Leu, Pro-Gly-Pro and Gly-Pro, Pro-Gly-Pro-Gly gives Pro-Gly-Pro and Gly-Pro, and Pro-Gly-Pro forms Gly-Pro.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::ff745aad672af1adf5c9a20c87486fd7 https://pubmed.ncbi.nlm.nih.gov/24397030 Zobrazit plný text záznamu