title: Purification and properties of beta-N-acetylglucosaminidase from Vibrio alginolyticus H-8.
abstract: Beta-N-acetylglucosaminidase [EC 3.2.1.30] from Vibrio alginolyticus H-8 was purified by column chromatography on DEAE-Sepharose FF, phenyl-Sepharose HP, Superdex 200HR, and Mono Q. The molecular weight of the enzyme was estimated by SDS-gel electrophoresis (SDS-PAGE) to be 75 kDa. The pI was 4.6. The activity was inhibited by Ag+, Hg2+, iodoacetate, p-chloromercuribenzoate, and N-ethylmaleimide.
authors.affiliation: United Graduate School of Agricultural Sciences, Gifu University, Shizuoka 422-8529 Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ohishi
authors.forename: K
authors.initials: K
authors.lastname: Murase
authors.forename: H
authors.initials: H
authors.lastname: Etoh