INFLUENCE OF SUBUNIT-SPECIFIC ANTIBODIES ON THE ACTIVITY OF THE F0 COMPLEX OF THE ATP SYNTHASE OF ESCHERICHIA-COLI .1. EFFECTS OF SUBUNIT B-SPECIFIC POLYCLONAL ANTIBODIES

Autor(en): DECKERSHEBESTREIT, G
SIMONI, RD
ALTENDORF, K 
Stichwörter: Biochemistry & Molecular Biology; F-0; F1F0; H+-ATPASE; MEMBRANE; POLAR LOOP REGION; PREDICTION; PROTON-TRANSLOCATING ATPASE; PURIFICATION; RECONSTITUTION; UNCF-PROTEIN
Erscheinungsdatum: 1992
Herausgeber: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Enthalten in: JOURNAL OF BIOLOGICAL CHEMISTRY
Band: 267
Ausgabe: 17
Startseite: 12364
Seitenende: 12369
Zusammenfassung: 
Incubation of F1-stripped everted membrane vesicles with antibodies against subunit b of the ATP synthase from Escherichia coli resulted in an inhibition of the binding of F1 to F0, whereas the proton translocation remained unaffected. Incubation of unstripped everted membrane vesicles with anti-b antibodies resulted in a partial loss of F1, and the remaining membrane-bound ATP-hydrolyzing activity is uncoupled from proton translocation. Similar results were obtained when F(ab')2 or Fab fragments were used. The immunoblot analysis of truncated b' subunits different in length showed that the antigenic determinants are located in the carboxyl-terminal half of the polypeptide chain.
ISSN: 00219258

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