LOCALIZATION OF THE POTASSIUM-ION ACTIVATION SITE IN HUMAN LIVER FRUCTOSE 1,6 - BISPHOSPHATASE

被引：6

作者：

XU, GJ ^{[1
]}

YU, ZB ^{[1
]}

HU, GF ^{[1
]}

CAO, HT ^{[1
]}

机构：

[1] ACAD SINICA,INST BIOPHYS,NATL LAB MACROMOLEC,BEIJING 100101,PEOPLES R CHINA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 194卷 / 03期

关键词：

D O I：

10.1006/bbrc.1993.1992

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Three mouse monoclonal antibodies of human liver fructose 1,6-bisphosphatase are shown to bind to the enzyme at different sites as determined by ELISA. The binding of one of the monoclonal antibodies, L2E1, mimics the effects of K+ ions, including increase in the enzyme activity and enhancement of the sensitivity of the enzyme to AMP inhibition. We tentatively suggest that human liver FruP2ase may have a specific K+ activation site, which at least partially overlaps with the L2E1 binding region. This site has been localized by analyzing the peptide fragments formed by cleavage with cyanogen bromide. © 1993 Academic Press, Inc.

引用

页码：1483 / 1490

页数：8

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