Purification and properties of aminopeptidase C from porcine skeletal muscle

1. 1. Aminopeptidase C was purified from porcine skeletal muscle. 2. 2. The mol. wt of the enzyme was found to be 103,000 on both Sephadex G-200 column chromatography and SDS-PAGE. 3. 3. The optimum pH for the hydrolysis of l-leucine p- nitroanilide was around 7.0. 4. 4. The activity of this enzyme...

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Veröffentlicht in:	COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY 1992-05, Vol.102 (1), p.129-135
Hauptverfasser:	Nishimura, Toshihide, Kato, Yutaka, Rhyu, Mee Ra, Okitani, Akihiro, Kato, Hiromichi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aminopeptidases - chemistry Aminopeptidases - isolation & purification Aminopeptidases - metabolism Animals Biochemistry & Molecular Biology Biological and medical sciences Fundamental and applied biological sciences. Psychology Hot Temperature Hydrogen-Ion Concentration Kinetics Life Sciences & Biomedicine Metals Molecular Sequence Data Molecular Weight Muscles - enzymology Oligopeptides - chemistry Science & Technology Striated muscle. Tendons Substrate Specificity Swine Vertebrates: osteoarticular system, musculoskeletal system Zoology
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Zusammenfassung:	1. 1. Aminopeptidase C was purified from porcine skeletal muscle. 2. 2. The mol. wt of the enzyme was found to be 103,000 on both Sephadex G-200 column chromatography and SDS-PAGE. 3. 3. The optimum pH for the hydrolysis of l-leucine p- nitroanilide was around 7.0. 4. 4. The activity of this enzyme was strongly inhibited by EDTA, bestatin and puromycin. 5. 5. The enzyme acted on the β-naphthylamide derivatives of amino acids and oligopeptides.
ISSN:	0305-0491 1096-4959 1879-1107
DOI:	10.1016/0305-0491(92)90284-X