Purification and properties of a dipeptidase from Streptococcus 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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آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولPurification and certain properties of a bacteriocin from Streptococcus mutans.
An inhibition factor from Streptococcus mutans strain C3603 (serotype c) was purified and isolated, and its properties indicated that it was a bacteriocin. Bacteriocin C3603 is a basic protein with a pI value of 10 and a molecular weight of 4,800. The activity of this bacteriocin was not affected by pH over a range of 1.0 to 12.0 or by storage at 100 degrees C for 10 min at pH 2.0 to 7.0 or sto...
متن کاملPurification and properties of pyruvate kinase from Streptococcus mutans.
Pyruvate kinase (EC 2.7.1.40) from Streptococcus mutans strain JC2 was purified, giving a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was 180,000 to 190,000, and the enzyme was considered to consist of four identical subunits. This enzyme was completely dependent on glucose 6-phosphate for activity, and the saturation curve...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1981
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.45.159