[SH-dependent aminopeptidase from bovine kidney. Isolation, physico-chemical properties and substrate specificity].
The SH-dependent aminopeptidase was isolated from bovine kidney and purified 800-fold. The enzyme has a pH optimum of 7.0 and pI of 5.5 and is activated by dithiothreitol and inhibited by p-chloromercurybenzoate. The enzyme has a molecular weight of 56000 and is represented by four polypeptide chains with m. w. of 14000. Aminopeptidase hydrolyzes beta-naphthylamides of arginine, alanine, leucine and proline and peptides with free N-terminal neutral and basic amino acid residues having L-configuration as well as angiotensin III. The enzyme does not split proteins, angiotensins I and II, B-chains of insulin and peptides with a blocked N-terminal amino group and peptides with proline as a second amino acid from the NH2-end.
D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity
D000626:Aminopeptidases; C036008:aminopeptidase, sulfhydryl dependent
SH-zavisimaia aminopeptidaza pochek byka. Vydelenie, fiziko-khimicheskie svoĭstva i substratnaia spetsifichnost'.