[Comparative characteristics of soluble and membrane brain aminopeptidases. I. Isolation, physico-chemical properties, catalytic activity].
The methods were worked out for isolating of the bovine brain soluble and membrane-bound aminopeptidases in highly purified state. One of the stages involved a biospecific-type chromatography on aminohexyl-Sepharose. Both enzymes were found to have equal molecular masses (ca. 100-107 kD) and isoelectric points (pI 4,6). None of the enzymes possessed a subunit structure. Both aminopeptidases were inactivated by omicron-phenanthroline and by an SH-reagent, p-hydroxymercuribenzoate. The catalytic constants for the hydrolysis of a specific substrate, L-leucine p-nitroanilide, were identical for the two enzymes. So far no differences in the physico-chemical or enzymatic properties of the soluble and membrane-bound enzymes were disclosed.
D000626:Aminopeptidases / Q000032:analysis / Q000302:isolation & purification*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D002417:Cattle; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008566:Membranes / Q000201:enzymology; D051379:Mice; D008970:Molecular Weight; D051381:Rats; D012995:Solubility; D013045:Species Specificity
D000626:Aminopeptidases
Sravnitel'naia kharakteristika rastvorimoĭ i membrannoĭ aminopeptidamozga. I. Vydelenie, fiziko-khimicheskie svoĭstva, kataliticheskaia aktivnost'.