PMID:1376322: Difference between revisions

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<span style = 'font-size: large'> '''Deckers-Hebestreit, G, Simoni, RD and Altendorf, K'''  (1992) Influence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies.''J. Biol. Chem.'' '''267''':12364-9</span>
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!align=left  |Citation
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'''Deckers-Hebestreit, G, Simoni, RD and Altendorf, K'''  (1992) Influence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies. ''J. Biol. Chem.'' '''267''':12364-9
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!align=left  |Abstract
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1376322 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || 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.
!align=left  |Keywords
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Adenosine Triphosphatases/metabolism; Antibodies/immunology; Blotting, Western; Epitopes/immunology; Escherichia coli/enzymology; Hydrolysis; Immunoglobulin Fab Fragments/immunology; Proton-Translocating ATPases/antagonists & inhibitors; Proton-Translocating ATPases/immunology; Proton-Translocating ATPases/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1376322 PubMed]
 
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
 
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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Latest revision as of 04:21, 15 September 2013

Citation

Deckers-Hebestreit, G, Simoni, RD and Altendorf, K (1992) Influence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies. J. Biol. Chem. 267:12364-9

Abstract

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.

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PubMed

Keywords

Adenosine Triphosphatases/metabolism; Antibodies/immunology; Blotting, Western; Epitopes/immunology; Escherichia coli/enzymology; Hydrolysis; Immunoglobulin Fab Fragments/immunology; Proton-Translocating ATPases/antagonists & inhibitors; Proton-Translocating ATPases/immunology; Proton-Translocating ATPases/metabolism

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