1999 Volume 22 Issue 8 Pages 866-869
This paper reports that β-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°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 it they were one of the components of this enzyme in the current study. The Km value of this enzyme was 92.3 μM and it was inhibited strongly by HgCl2 and sodium dodecyl sulfate (SDS).
