PH DEPENDENT CONFORMATIONAL-CHANGES MODULATE FUNCTIONAL-ACTIVITY OF THE MITOCHONDRIAL ATPASE INHIBITOR PROTEIN

被引：17

作者：

SAH, JF ^{[1
]}

KUMAR, C ^{[1
]}

MOHANTY, P ^{[1
]}

机构：

[1] JAWAHARLAL NEHRU UNIV,SCH LIFE SCI,BIOENERGET LAB,NEW DELHI 110067,INDIA

来源：

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

关键词：

D O I：

10.1006/bbrc.1993.1997

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：

A 12kDa, heat stable protein (IF1) inhibiting hydrolytic activity of submitochondrial particles was purified to electrophoretic homogeneity from buffalo heart mitochondria. Specific activity of the purified fraction was >5000 units/mg. Maximal inhibition was observed at pH 6.0 and was Mg++ and ATP dependent. Circular dichroism studies showed that the inhibitor peptide undergoes a dramatic, reversible conformational change in response to pH which correlates well with its ability to inhibit ATP hydrolysis catalyzed by inhibitor depleted submitochondrial particles. It is shown for the first time that IF1 with a predominantly β-sheet component is more efficient at suppressing ATPase activity. © 1993 Academic Press, Inc.

引用

页码：1521 / 1528

页数：8

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