Purification and characterization of endo-.BETA.-N-acetylglucosaminidase from a Flavobacterium sp.
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چکیده
منابع مشابه
Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli.
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...
متن کاملPurification , Characterization and Gefie from Enterobacter sp . G - 1 Analysis of N - Acetylglucosaminidase
Enterobacter sp. G-1 is a bacterium isolated preyiously as a chitinase-preducing bacterium. We found this bacterium also produced IVLacetylglucesaminidase and characterized that in this study. Extracellular IVLacetylglucosaminidase of 92.0kDa was purified near hemogeneity by 8.57-fold from Enterobacter sp. G-1. The eptirn-m temperature and the optimum pH of the purified iVLacetylglucosaminidase...
متن کاملPurification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.
The DNA region encoding the mature form of a pneumococcal murein hydrolase (LytB) was cloned and expressed in Escherichia coli. LytB was purified by affinity chromatography, and its activity was suggested to be the first identified endo-beta-N-acetylglucosaminidase of Streptococcus pneumoniae. LytB can remove a maximum of only 25% of the radioactivity from [(3)H]choline-labeled pneumococcal cel...
متن کاملBacteriolytic enzymes from Staphylococcus aureus. Specificity of ction of endo-beta-N-acetylglucosaminidase.
The bacteriolytic enzyme with an isoelectric point of 9.5 that is produced by all strains of Staphylococcus aureus investigated was purified from strain M18 (Wadström & Hisatsune, 1970). This enzyme released reducing groups from cell walls of Micrococcus lysodeikticus and was thus shown to be a bacteriolytic hexosaminidase. Although dinitrophenylation and acid hydrolysis of cell walls hydrolyse...
متن کاملPurification 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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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1986
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.50.421