Purificationand Properties of Aminopeptidase C Chicken Sketetal Muscle from
نویسندگان
چکیده
Aminopeptidase C was purified from fresh chicken skeletal muscle by arnmonium sulfate fract;onation,andbysuccessivechromatographyonDEAE-cellulose,UltrogelAcA34,DEAE-cellulose again, and an alanine AH-Sepharose 4B ftMnity column twice. The purificd enzyme migrated as a s;ngle band by SDS-PAGE. Am;nopeptidase C was purified about 300-fo1cl over the crllde extraet with a },ield of O.6%. The molecular weight of this enzyme was found to be 18S,OOO by get filtration in a Sepharose 6B colllmn a"d 9Z,OOO by SDS-PAGE. The optimum pH for thc hydrolysis of L,-lellcine fi-naphthylamide wfts 6.0-7.e, the enzyme being stab[e in the range of pH 6.5-8.0. The aetivity of this enzyme was strongly inhibited by, EDTA and p"romycin, and was high against the fi-naphthylamide deriyatiyes of I.ys, Lell, Ala and Met. The enzyme was mere actiye towards triand tetrapeptides than towards dipeptides.
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