Chitin synthesis in Mucor rouxii

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Properties of a particulate chitin synthetase from Mucor rouxii.

The properties and behavior of a “microsomal” (100,000 X g particles) chitin synthetase of Mucor rouxii were investigated. The enzyme utilizes uridine diphosphate N-acetylD-glucosamine (UDP-GlcNAc) as glycosyl donor and is strongly and specifically activated by free N-acetyl-o-glucosamine (GlcNAc). A variety of GlcNAc analogues were tested as activators but were found ineffective. A small propo...

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Isolation of chitin deacetylase from Mucor rouxii by immunoaffinity chromatography

The purification of chitin deacetylase from Mucor rouxii to homogeneity employing conventional methods has already been described. However, a lengthy protocol is required resulting in a low yield and specific activity for the enzyme . A 169-fold one-step purification of chitin deacetylase by immunoaffinity chromatography is reported, resulting in a homogeneous enzyme preparation. The enzyme pur...

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Bioconversion of chitin to chitosan: purification and characterization of chitin deacetylase from Mucor rouxii.

Chitin deacetylase, the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetylglucosamine in chitin, has been purified to homogeneity from mycelial extracts of the fungus Mucor rouxii and further characterized. The enzyme exhibits a low pI (approximately 3). Its apparent molecular mass was determined to be approximately 75 kDa by sodium dodecyl sulfate/polyacrylamide gel electroph...

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Properties of Chitin Synthetase in Isolated Chitosomes from Yeast Cells of Mucor rouxii*

Chitin synthetase was isolated and purified 120-fold from the supernatant fraction (54,500 x g) of broken yeast cells of Mucor rouxii. The purified preparations consisted mainly of chitin synthetase particles (chitosomes) with an average size larger than 7 x 10” daltons (by gel filtration) and an average sedimentation coefficient of 105 S. The samples also contained other enzyme complexes (fatt...

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Properties of chitin synthetase in isolated chitosomes from yeast cells of Mucor rouxii.

Chitin synthetase was isolated and purified 120-fold from the supernatant fraction (54,500 X g) of broken yeast cells of Mucor rouxii. The purified preparations consisted mainly of chitin synthetase particles (chitosomes) with an average size larger than 7 X 10(6) daltons (by gel filtration) and an average sedimentation coefficient of 105 S. The samples also contained other enzyme complexes (fa...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1970

ISSN: 0306-3283

DOI: 10.1042/bj1190011pa