منابع مشابه
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. ...
متن کاملMutant of Bacillus subtilis lacking exo-beta-N-acetylglucosaminidase activity.
A procedure for the isolation of exo-beta-N-acetylglucosaminidase mutants, by using a plate assay method incorporating a fluorescent substrate, has been developed. A mutant lacking exo-beta-N-acetylglucosaminidase activity has been isolated and shown to grow, divide, autolyze, and sporulate as well as the parental strain.
متن کاملPurification 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 کاملCharacterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.
A gene encoding a putative peptidoglycan hydrolase, named acmB, which is a paralogue of the major autolysin acmA gene, was identified in the Lactococcus lactis genome sequence. The acmB gene is transcribed in L. lactis MG1363 and its expression is modulated during cellular growth. The encoded AcmB protein has a modular structure with three domains: an N-terminal domain, especially rich in Ser, ...
متن کاملRole of N-acetylglucosaminidase and N-acetylmuramidase activities in Enterococcus faecalis peptidoglycan metabolism.
Identification of the full complement of peptidoglycan hydrolases detected by zymogram in Enterococcus faecalis extracts led to the characterization of two novel hydrolases that we named AtlB and AtlC. Both enzymes have a similar modular organization comprising a central catalytic domain fused to two LysM peptidoglycan-binding modules. AtlB and AtlC displayed N-acetylmuramidase activity, as dem...
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ژورنال
عنوان ژورنال: Journal of Experimental Medicine
سال: 1968
ISSN: 1540-9538,0022-1007
DOI: 10.1084/jem.127.4.833