title: Purification and properties of aminopeptidase C from porcine skeletal muscle.
abstract: 1. Aminopeptidase C was purified from porcine skeletal muscle. 2. The mol. wt of the enzyme was found to be 103,000 on both Sephadex G-200 column chromatography and SDS-PAGE. 3. The optimum pH for the hydrolysis of L-leucine p-nitroanilide was around 7.0. 4. The activity of this enzyme was strongly inhibited by EDTA, bestatin and puromycin. 5. The enzyme acted on the beta-naphthylamide derivatives of amino acids and oligopeptides.
authors.affiliation: Department of Agricultural Chemistry, University of Tokyo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nishimura
authors.forename: Y
authors.initials: Y
authors.lastname: Kato
authors.forename: M R
authors.initials: MR
authors.lastname: Rhyu
authors.forename: A
authors.initials: A
authors.lastname: Okitani
authors.forename: H
authors.initials: H
authors.lastname: Kato
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008670:Metals; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009842:Oligopeptides / Q000737:chemistry; D013379:Substrate Specificity; D013552:Swine
chemical_list: D008670:Metals; D009842:Oligopeptides; D000626:Aminopeptidases; C072222:aminopeptidase C