Trinitrophenyl-ATP and -ADP bind to a single nucleotide site on isolated β-subunit of Escherichia coli F1-ATPase. In vitro assembly of F1-subunits requires occupancy of the nucleotide-binding site on β-subunit by nucleoside triphosphate

Journal of Biological Chemistry

Volumn 263, Issue 12, 1988, Pages 5569-5573

  Rao, R ^a   Al Shawi, M K ^a   Senior, A E ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; BINDING SITES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GUANOSINE TRIPHOSPHATE; HYDROGEN-ION CONCENTRATION; INOSINE TRIPHOSPHATE; MACROMOLECULAR SYSTEMS; PROTON-TRANSLOCATING ATPASES; SPECTROMETRY, FLUORESCENCE; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0023879516     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)