Inhibition by bestatin of a mouse ascites tumor dipeptidase

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Purification and properties of a mouse ascites tumor dipeptidase, a metalloenzyme.

A dipeptidase that hydrolyzes L-Ala-Gly and a wide spectrum of other L-ar-dipeptides has been purified 800-fold from the soluble fraction of Ehrlich-LettrB mouse actesis tmnor cells. The highest specific activity (micromoles of dipeptide hydrolyzed at 40” per min per mg of protein) achieved was 2,600 with Ala-Gly, the substrate with which purification was followed. With the best substrate, Ala-...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)83142-8