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Volumn 1556, Issue 2-3, 2002, Pages 133-141
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Dimerization of F0F1ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF1
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Author keywords
Blue native polyacrylamide electrophoresis; Dimerization; Histochemical staining; Inhibitor protein IF1; Mitochondrial F0F1ATPsynthase
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Indexed keywords
DIMER;
MONOMER;
PROTEIN ANTIBODY;
PROTEIN INHIBITOR;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;
TRITON X 100;
ADENOSINE TRIPHOSPHATE;
ENZYME INHIBITOR;
MULTIENZYME COMPLEX;
PROTEIN SUBUNIT;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;
ANIMAL CELL;
ARTICLE;
CONTROLLED STUDY;
DIMERIZATION;
ENERGY;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME STRUCTURE;
EXTRACTION;
HEART MITOCHONDRION;
HISTOCHEMISTRY;
IMMUNOBLOTTING;
NONHUMAN;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN FUNCTION;
PROTEIN PROTEIN INTERACTION;
SOLUBILIZATION;
ANIMAL;
CATTLE;
CHEMISTRY;
DRUG ANTAGONISM;
ENZYMOLOGY;
METABOLISM;
PROTEIN BINDING;
BOVINAE;
ADENOSINE TRIPHOSPHATE;
ANIMALS;
CATTLE;
DIMERIZATION;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME INHIBITORS;
MITOCHONDRIA, HEART;
MULTIENZYME COMPLEXES;
PROTEIN BINDING;
PROTEIN SUBUNITS;
PROTON-TRANSLOCATING ATPASES;
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EID: 0037010590
PISSN: 00052728
EISSN: None
Source Type: Journal
DOI: 10.1016/S0005-2728(02)00344-4 Document Type: Article |
Times cited : (61)
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References (33)
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