Purification and Properties of a Dipeptidase fromStreptococcus cremoris
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چکیده
منابع مشابه
Purification 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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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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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: Agricultural and Biological Chemistry
سال: 1981
ISSN: 0002-1369
DOI: 10.1080/00021369.1981.10864481