Purification of vacuoles from Neurospora crassa.
نویسندگان
چکیده
منابع مشابه
The purification and properties of superoxide dismutase from Neurospora crassa.
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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Extracellular Neurospora laccase (p-diphenol:oxygen oxidoreductase; EC 1.10.3.2) has been purified to apparent homogeneity by classical purification techniques. The enzyme, which consists of mainly one form, has a molecular weight of 64,800 and contains 11% carbohydrate. The ultraviolet, visible, and electron paramagnetic resonance spectra indicate that both type I and type II copper are presen...
متن کاملPurification 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...
متن کاملThe purification and properties of histidinol dehydrogenase from Neurospora crassa.
1. A procedure is described for the purification of l-histidinol dehydrogenase (l-histidinol-NAD oxidoreductase, EC 1.1.1.23) from Neurospora crassa. 2. The enzyme, as purified, has a sedimentation coefficient, S(20), of 7.1s and a molecular weight of 81 000. Considerable variation is possible in the state of polymerization of the enzyme, giving rise to observed molecular weights from 40 000 to...
متن کاملPurification and characterization of flavokinase from Neurospora crassa.
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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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1981
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.1.9.797