Purification and Characterization ofβ-N-Acetylglucosaminidase fromAlteromonassp. Strain O-7

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Molecular cloning of the gene which encodes beta-N-acetylglucosaminidase from a marine bacterium, Alteromonas sp. strain O-7.

The gene encoding the periplasmic beta-N-acetylglucosaminidase (GlcNAcase B) from a marine Alteromonas sp. strain, O-7, was cloned and sequenced. The protein sequence of GlcNAcase B revealed a highly significant homology with Vibrio GlcNAcase and alpha- and beta-chains of human beta-hexosaminidase.

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Purification , 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...

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Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.

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Intraphagocytic Β-n-acetylglucosaminidase

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. ...

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ژورنال

عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry

سال: 1995

ISSN: 0916-8451,1347-6947

DOI: 10.1271/bbb.59.1135