Properties of partially purified beta-N-acetylglucosaminidase from bovine crystalline lens.
This paper reports that beta-N-acetylglucosaminidase from bovine lens has potent enzyme activity compared with other glycosidases in the lens. The partially purified enzyme was used to determine its physiological properties. The optimal pH and optimal temperature of this enzyme was approximately 6.3 and 40 degrees C, respectively. The apparent native molecular weight of this enzyme obtained by gel filtration chromatography was 540 kDa. Furthermore, the enzyme fraction contained 3 polypeptides with molecular weights of 28.8, 28.0 and 26.0 kDa, although it is not certain if they were one of the components of this enzyme in the current study. The Km value of this enzyme was 92.3 microM and it was inhibited strongly by HgCl2 and sodium dodecyl sulfate (SDS).
Kamei
A
A
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University, Nagoya-shi, Aichi-ken, Japan.
Hayashi
S
S
D000118:Acetylglucosaminidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology*
D004791:Enzyme Inhibitors; D000118:Acetylglucosaminidase