ESTIMATION OF H+-TRANSLOCATION STOICHIOMETRY OF MITOCHONDRIAL ATPASE BY COMPARISON OF PROTON-MOTIVE FORCES WITH CLAMPED PHOSPHORYLATION POTENTIALS IN SUB-MITOCHONDRIAL PARTICLES

被引：20

作者：

SORGATO, MC

GALIAZZO, F

PANATO, L

FERGUSON, SJ

机构：

[1] UNIV PADUA,IST CHIM BIOL,I-35100 PADUA,ITALY

[2] UNIV BIRMINGHAM,DEPT BIOCHEM,BIRMINGHAM B15 2TT,W MIDLANDS,ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1982年 / 682卷 / 01期

关键词：

D O I：

10.1016/0005-2728(82)90133-5

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：

引用

页码：184 / 188

页数：5

共 21 条

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[6] THE PROTON-PER-ELECTRON STOICHIOMETRY OF SITE-1 OF OXIDATIVE-PHOSPHORYLATION AT HIGH PROTONMOTIVE FORCE IS CLOSE TO 1.5
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[8] ADENOSINE TRIPHOSPHATASE-INHIBITOR CONTENT OF BOVINE HEART SUBMITOCHONDRIAL PARTICLES - INFLUENCE OF INHIBITOR ON ADENOSINE TRIPHOSPHATE-DEPENDENT REACTIONS
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[10] SPECIFICITY OF NUCLEOTIDE BINDING AND COUPLED REACTIONS UTILIZING MITOCHONDRIAL ATPASE
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