Enzyme purification by electrodecantation
نویسندگان
چکیده
منابع مشابه
Selective enzyme purification by affinity chromatography.
The purification of proteins by conventional procedures is frequently laborious and incomplete, and the yields are often low. Enzyme isolation based on a highly specific biological property-strong reversible association with specific substrates or inhibitors-has received only limited attention.‘-’ In affinity chromatography, the enzyme to be purified is passed through a column containing a cros...
متن کاملPurification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei
Milk clotting enzyme (M CE) produced by: Rhizomucor miehei was purified and characterized.The enzyme was purified 220.29-fold with specific activity about 14444.2 U/mg protein byultrafiltration, ammonium sulfate fractionation, Sephacryl S-300 chromatography. The maximumenzyme activity was at 65°C.The milk clotting activity was decreased steadily as pH is increased and indicated maximumactivity ...
متن کاملOptimal Conditions for Extraction and Purification of Penicillinase Enzyme
Background and Objective: The present study aimed to evaluate the optimum conditions for extracting and purifying penicillinase enzyme. The enzyme source was Bacillus licheniformis 6346 obtained from the Iranian Research Organization for Science and Technology. Materials and Methods: B. licheniformis was cultured in a medium containing mineral salts, nitrogen compounds, and cultured carbon sou...
متن کاملPost - proline Cleaving Enzyme PURIFICATION
The endopeptidase, post-proline cleaving enzyme, has been purified 10,500-fold in an overall yield of 18% from lamb kidney. The enzyme possesses a specific activity of 45 ~mol/mg/min as tested with the substrate Z-Gly-Pro-Leu-Gly (K,,, = 6.0 x 10m5), has a molecular weight of 115,000, is comprised of two subunits with a molecular weight of 57,000, and exhibits maximal activity at pH 7.5 to 8.0....
متن کاملPurification and properties of the enzyme chondroitinase.
The enzymatic degradation of chondroitin sulfuric acid can be catalyzed by purified bovine testicular hyaluronidase (1, 2) and by an enzyme preparation from Flavobacterium heparinum (3). Dodgson and Lloyd (4) obtained a chondroitinase from Proteus vulgaris that converted chondroitin sulfuric acid to the disaccharide, N-acetylchondrosin sulfate. Previous work from this laboratory (5) has confirm...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1210161