Properties of Partially Purified β-N-Acetylglucosaminidase from Bovine Crystalline Lens
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概要
- 論文の詳細を見る
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℃, 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 K_m value of this enzyme was 92.3 μM and it was inhibited strongly by HgCl_2 and sodium dodecyl sulfate (SDS).
- 公益社団法人日本薬学会の論文
- 1999-08-15
著者
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KAMEI Akira
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University
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Kamei Akira
Department Of Biochemistry Faculty Of Pharmaceutical Sciences Meijo University
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Hayashi S
Graduate School Of Pharmaceutical Sciences Osaka University
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HAYASHI Sayoko
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University
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