Solubilization of adenosine triphosphatase from membranes of Escherichia coli: effect of p-aminobenzamidine.
AUTOR(ES)
Downie, J A
RESUMO
The five subunits of the membrane-bound adenosine triphosphatase (F1) from Escherichia coli were identified on electrophoretograms of membranes which had been washed with a low-ionic-strength buffer containing the protease inhibitor p-aminobenzamidine. All of the subunits of the membrane-bound F1 appeared to have the same molecular weights and isoelectric points as those of the soluble F1, as judged by two-dimensional electrophoresis. p-Aminobenzamidine inhibited the solubilization of F1 rebound to F1-depleted membranes, and was found to inhibit the membrane-bound adenosine triphosphatase activity to a much greater extent than the solubilized activity. It is therefore unlikely that p-aminobenzamidine inhibits the solubilization of F1 by inhibiting a protease, as suggested previously by Cox et al. (G.B. Cox, J.A. Downie, D.R.H. Fayle, F. Gibson, and J. Radik, J. Bacteriol. 133:287--292, 1978).
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=218241Documentos Relacionados
- Energy-Transducing Adenosine Triphosphatase from Escherichia coli: Purification, Properties, and Inhibition by Antibody
- Membrane Adenosine Triphosphatase of Escherichia coli: Activation by Calcium Ion and Inhibition by Monovalent Cations1
- Adenosine Triphosphatase Activity of Mycoplasma Membranes1
- Effect of Membrane Lipid Composition on the Allosteric Inhibition by Sodium of the (Ca2+)-Adenosine Triphosphatase from Escherichia coli
- Inhibition, by a protease inhibitor, of the solubilization of the F1-portion of the Mg2+-stimulated adenosine triphosphatase of Escherichia coli.