PURIFICATION AND CHARACTERIZATION OF GLYOXALASE-I FROM HANSENULA-MRAKII

被引:14
作者
INOUE, Y [1 ]
TRAN, LT [1 ]
YOSHIKAWA, K [1 ]
MURATA, K [1 ]
KIMURA, A [1 ]
机构
[1] KYOTO UNIV,FOOD SCI RES INST,UJI,KYOTO 611,JAPAN
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1991年 / 71卷 / 02期
关键词
D O I
10.1016/0922-338X(91)90239-D
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Glyoxalase I was purified from Hansenula mrakii IFO 0895 which was resistant to 25 mM methyglyoxal. The molecular weight of the purified enzyme was calculated to be 38,000 by both gel-filtration of Sephadex G-150 and SDS-PAGE. The enzyme was almost specific to methylglyoxal (K(m) = 0.91 mM). The activity of the enzyme was not inhibited by metal ion chelators such as EDTA, which is a potent inhibitor for glyoxalase Is from other sources.
引用
收藏
页码:131 / 133
页数:3
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