Purification and Properties of a Mouse Ascites Tumor Dipeptidase, a Metalloenzyme
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منابع مشابه
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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Interferon production was induced in mouse Ehrlich ascites tumor cells by infection with Newcastle disease virus. The interferon produced was purified by precipitation with ammonium sulfate, chromatography on carboxymethyl-Sephadex, treatment with blue dextran and polyethylene glycol, gel filtration on Bio-Gel P-60 and Bio-Gel P-200, chromatography on phosphocellulose, isoelectric focusing, and...
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A peptidase from Escherichia coli B has been prepared in a highly pure form and characterized with respect to its substrate specificity, requirements for activity, size and subunit structure. This enzyme preferentially catalyzes the hydrolysis of certain methionyl dipeptides and for this reason is referred to as dipeptidase M. Of the substrates tested with the homogeneous enzyme methionylalanin...
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15 صفحه اولPurification and Characterization of a Dipeptidase from Streptococcus cremoris Wg2.
A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 49,000. The dipeptidase is capable of hydrolyzing a range of dipeptides, ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62465-2