Kinetic 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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In Streptococcus lactis ML3 and Streptococcus cremoris Wg2 the uptake of glutamate and glutamine is mediated by the same transport system, which has a 30-fold higher affinity for glutamine than for glutamate at pH 6.0. The apparent affinity constant for transport (KT) of glutamine is 2.5 +/- 0.3 microM, independent of the extracellular pH. The KTS for glutamate uptake are 3.5, 11.2, 77, and 120...
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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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The procedure for the purification of renal dipeptidase from particulate kidney cortex fractions has been modified to eliminate a time-consuming washing process and a chromatographic step which frequently led to loss in activity. The over-all purification resulted in the isolation of 5.8 mg of purified peptidase from 1.5 kg of kidney cortex and produced an enzyme approximately 500 times more ac...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1982
ISSN: 0002-1369
DOI: 10.1080/00021369.1982.10865544