SUBSTRATE-SPECIFICITY AND POSITIONAL PREFERENCE OF A LIPOPROTEIN-LIPASE

被引:4
作者
KHEIROLOMOOM, A [1 ]
YOSHIDA, KI [1 ]
KATOH, S [1 ]
SADA, E [1 ]
机构
[1] KYOTO UNIV,DEPT CHEM ENGN,SAKYO KU,KYOTO 606,JAPAN
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1992年 / 73卷 / 05期
关键词
D O I
10.1016/0922-338X(92)90287-5
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 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];
摘要
The substrate specificity and positional preference of a membrane-bound lipoprotein lipase with and without reconstitution in liposomes were studied. The enzyme showed the same preference for the acyl groups in the 1- and 3-positions of triglycerides, while its activity toward the 2-position was one-third of that toward the 1- or 3-positions. The substrate specificity of the enzyme toward fatty acids of different chain length and degree of unsaturation was in the order of C:14>C:16>C:18:1greater-than-or-equal-toC:18. The enzyme with and without reconstitution showed the same positional preference and substrate specificity.
引用
收藏
页码:403 / 404
页数:2
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