Alkaline protease from Neurospora crassa. Purification and partial characterization.
نویسندگان
چکیده
منابع مشابه
Purification and characterization of arginase from Neurospora crassa.
We have purified an enzymatically active form of arginase from a wild-type strain of Neurospora crassa to homogeneity. The enzyme has a subunit molecular weight of 38,300 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The native protein migrated as a hexamer during gel-filtration chromatography with an apparent molecular weight of 266,000. The enzyme exhibited hyper...
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The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) prot...
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The ATP-dependent phosphorylation of riboflavin to FMN by flavokinase is the key step in flavin biosynthesis. Flavokinase has been purified from a fungal source for the first time. The enzyme purified from a cell wall lacking mutant of Neurospora crassa, slime, is a monomer of M(r) 35.5 kDa with maximal activity at alkaline pH and high temperature (55 degrees C). The K(m) for both substrates is...
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Bacillus isolates were analyzed for alkaline protease production on casein containing agar plates and identified by clear zones of casein hydrolysis around colonies. Two gram positive Bacillus isolates S5 and C3 which showed the best enzyme production were studied for purification by precipitation and dialysis. The intracellular alkaline protease enzyme was purified about 4 fold with a yield of...
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Soluble extracts of Neurospora crassa contain a single, electrophoretically distinct, superoxide dismutase. This enzyme has been isolated and has been found to be a bluegreen, copperand zinc-containing enzyme, similar to that already described from bovine tissues and from garden peas. The molecular weight was ,approximately 31,000, and the enzyme appeared to be composed of 2 subunits of equal s...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70049-0