Purification and properties of beta-N-acetylglucosaminidase from Vibrio alginolyticus H-8

Authors
Ohishi, K Murase, K Etoh, H
Citation
K. Ohishi et al., Purification and properties of beta-N-acetylglucosaminidase from Vibrio alginolyticus H-8, J BIOSCI BI, 88(1), 1999, pp. 98-99
Citations number
7
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723 → ACNP
Volume
88
Issue
1
Year of publication
1999
Pages
98 - 99
Database
ISI
SICI code
1389-1723(199907)88:1<98:PAPOBF>2.0.ZU;2-S
Abstract
beta-N-Acetylglucosaminidase [EC 3.2.1.30] from Vibrio alginolyticus H-8 wa s purified by column chromatography on DEAE-Sepharose FF, phenyl-Sepharose HP, Superdex 200HR, and Mono Q. The molecular weight of the enzyme was esti mated by SDS-gel electrophoresis (SDS-PAGE) to be 75 kDa. The pI was 4.6. T he activity was inhibited by Ag+, Hg2+, iodoacetate, p-chloromercuribenzoat e, and N-ethylmaleimide.