The N-termini of the α and β subunits at the top of F1 stabilize the energy-transfer function in the mitochondrial F1F(o) ATP synthase

European Journal of Biochemistry

Volumn 252, Issue 1, 1998, Pages 155-161

  Xu, Ting ^a   Candita, Cosimo ^a   Amoruso, Giovanna ^a   Papa, Sergio ^a  

^a UNIVERSITY OF BARI   (Italy)

Author keywords

ATP synthase; Energy coupling; F(o)F1 reconstitution; F1; Trypsin digestion

Indexed keywords

AMINO ACID; DICYCLOHEXYLCARBODIIMIDE; GUANOSINE TRIPHOSPHATE; OLIGOMYCIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPSIN;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CATALYSIS; ELECTROPHORESIS; ENZYME ACTIVITY; HYDROLYSIS; IMMUNOBLOTTING; MITOCHONDRIAL ENERGY TRANSFER; PRIORITY JOURNAL; PROTON MOTIVE FORCE; PROTON TRANSPORT; SEQUENCE ANALYSIS;

ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CATTLE; DICYCLOHEXYLCARBODIIMIDE; FLUORESCENT DYES; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; KINETICS; MITOCHONDRIA, HEART; MOLECULAR SEQUENCE DATA; OLIGOMYCINS; PEPTIDE FRAGMENTS; PROTON-TRANSLOCATING ATPASES; PROTONS; SEQUENCE ANALYSIS; TRYPSIN; UREA;

EID: 0032520090     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520155.x     Document Type: Article

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