Purification and Properties of an Endo-β-N-acetylglucosaminidase from Streptomyces griseus
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Purification and Properties of an Endo-P-iv-acetylglucosaminidase
An enzyme that hydrolyzes di-N-acetylchitobiose linkages in oligosaccharides and glycoproteins was purified to homogeneity from cultural filtrates of Streptomyces griseus. The molecular weight of the enzyme, determined by sedimentation equilibrium analysis, is 27,200 f ZOO, and it appears to consist of a single polypeptide chain. This apparent endo/3-N-acetylglucosaminidase was completely stabl...
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beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular weight of this enzyme, determined by bo...
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Endo-β-N-acetylglucosaminidase (ENGase), which catalyzes hydrolysis of N-linked oligosaccharides, is a useful tool for analyzing oligosaccharide contents of glycoproteins. However, there are only a few known ENGases that can catalyze the hydrolysis of human complex type oligosaccharides, and although commercially available, they are expensive. Here, we report the cloning of two ENGase encoding ...
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The beta-N-acetylglucosaminidases of rabbit and human polymorphonuclear leukocytes and of rabbit alveolar macrophages have been studied in comparison with the beta-N-acetylglucosaminidase derived from a soil bacillus which had previously been shown to hydrolyze the group-specific polysaccharide of Group A streptococci. The phagocytic enzymes are lysosome associated and have an acid pH optimum. ...
متن کاملPurification and some properties of protease I having transfer action from Streptomyces griseus var. alcalophilus.
Streptomyces griseus var. alcalophilus was selected because it secreted a unique protease (protease I) that catalyzed the transfer reaction forming the hydroxamic acids of various amino acids. Protease I was purified to the electrophoretically homogeneous state and an activity of more than 125-fold that of the culture broth. The molecular weight of the enzyme was estimated to be 25,000 by gel f...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43001-9