Alanyl aminopeptidase of bovine seminal vesicle secretion.
Multiple forms of an aminopeptidase hydrolysing L-alanine- and various other amino acid-beta-naphthylamides in bovine seminal vesicle secretion were studied after fractionation on gel filtration, anion exchange chromatography and chromatofocusing. Two forms of the enzyme were found in all these fractionations: one with a high molecular weight was aggregated or particle-bound and the other had a molecular weight of about 237,000. The high-molecular-weight form dissociated with Triton X-100 via an intermediate into the basic enzyme form with concurrent change in the pI and anionic sites. The basic form of the enzyme differed from the high-molecular-weight forms in substrate preference, response to some modifiers, thermal stability and kinetic constants.
D000410:Alanine Transaminase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008297:Male; D012669:Seminal Vesicles / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity
D007527:Isoenzymes; D000410:Alanine Transaminase