Thermostable proteinases from a luminous bacterium, Vibrio logei strain CPM-D3. Purification and some properties.
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چکیده
منابع مشابه
Purification and some properties of a thermostable metal proteinase produced by Thermomicrobium sp. KN-22 strain.
An extreme thermophile that produces a heat-stable proteinase was isolated from hot-spring water and classified as Thermomicrobium sp. KN-22 (growth temperature, 50-83 degrees C; and optimum growth temperature, 70 degrees C). The proteinase was purified from the culture broth of this strain by fractionation with ammonium sulfate, chromatography on columns of DEAE-cellulose and CM-Sepharose CL-6...
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Two proteinases (proteinases I and II) have been purified from Crotalus adamanteus venom to the stage of electrophoretic homogeneity and proteinase II has been crystallized. The proteinases differ slightly in molecular weight and amino acid composition. Both are metalloenzymes requiring Zn2+ or Ca2+, or both; neither requires thiol compounds for activation. The proteinases are free of esterolyt...
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Previous investigations have shown that members of the genus Vibrio possess a novel enzyme activity decarboxylating L-2,4-diaminobutyric acid (DABA) to 1,3-diaminopropane (DAP). In this paper we describe the purification, by about 3600-fold, of the enzyme from V. alginolyticus. The purified enzyme was apparently homogeneous, and had a specific activity of 4200 nmol DAP min-1 (mg protein)-1. The...
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ژورنال
عنوان ژورنال: Chemical and Pharmaceutical Bulletin
سال: 1990
ISSN: 0009-2363,1347-5223
DOI: 10.1248/cpb.38.1644