| STUDY OF ${beta}$-GLUCURONIDASE FROM SULL SEMINAL PLASMA:PURIFICATION AND PROPERTIES |
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Chul-Hak Yang1, Hee-Yong Lee2 |
1Dept. of Chemistry, College of Natural Sciences Seoul National University
2Dept. of Urology, College of Medicine, Seoul National University |
| 황소의 정액에서 베타-굴룩 유로니다아제의 정제 및 그 성질에 관한 연구 |
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양철학1, 이희영2 |
1서울대학교 자연과학대학화학과
2서울대학교 의과대학 비뇨기과학교실 |
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| Abstract |
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${\beta}$-Glucuronidase from bull seminal plasma was partially purified by $(NH_4)_2SO_4$fractionation, two successive DEAE-cellulose columns, isoelectric focusing (pH 4 to 6) and Gel filtration on Sephadex G-200. Only one form of ${\beta}$-glucuronidase was obtained by isoelectric focusing at pH 5.13. Highly purified ${\beta}$-glucuronidase had specific activity of 34 units/mg protein and showed one major and some minor contaminants by disc gelk electrophoresis. The enzyme showed maximum activity at pH 5.2 and at $48^{\circ}C$. The enzyme was completely inhibited by 1,4 saccharo-${\alpha}$-lactone (5 mM). Albumin and 0.15 M NaCl increased the ${\beta}$-glucuronidase activity. Km of ${\beta}$-glucuronidase using phenolphthalein mono-${\beta}$-glucuronic acid as substrate was 2.9 mM and Vmax was $0.8{\mu}$mole/min. The enzyme appeared to be a glycoprotein by its binding to concanvalin |
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