Purification and properties of aminopeptidase C from porcine skeletal muscle.
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.
Nishimura
T
T
Department of Agricultural Chemistry, University of Tokyo, Japan.
Kato
Y
Y
Rhyu
M R
MR
Okitani
A
A
Kato
H
H
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
D008670:Metals; D009842:Oligopeptides; D000626:Aminopeptidases; C072222:aminopeptidase C