FSBA modifies both α- and β-subunits of F1 specifically and can be bound together with AXP at the same α-subunit

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1318, Issue 1-2, 1997, Pages 107-122

  Hartog, A F ^a   Edel, C M ^a   Braham, J ^a   Muijsers, A O ^a   Berden, J A ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

Adenosine binding pocket; Anion binding site; F1 ATPase; Non catalytic site; Regulatory site

Indexed keywords

ADENOSINE DERIVATIVE; ADENOSINE TRIPHOSPHATASE; INOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CATTLE; ENZYME BINDING; ENZYME INHIBITION; ENZYME SUBUNIT; GEL ELECTROPHORESIS; HEART; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IN VITRO STUDY; ISOTOPE LABELING; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

ADENINE NUCLEOTIDES; ADENOSINE; AFFINITY LABELS; ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CATTLE; DIPHOSPHATES; ENZYME INHIBITORS; KINETICS; MITOCHONDRIA, HEART; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; PYROPHOSPHATASES;

ANIMALIA; BOS TAURUS;

EID: 0031037061     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(96)00110-7     Document Type: Article

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