This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cox, G B Articles by Radik, J Search for Related Content PubMed PubMed Citation Articles by Cox, G B Articles by Radik, J

Inhibition, by a protease inhibitor, of the solubilization of the F1-portion of the Mg2+-stimulated adenosine triphosphatase of Escherichia coli.

ABSTRACT

The effects of two protease inhibitors on the solubilization of the membrane-bound Mg2+-adenosine triphosphatase (Mg-ATPase) of Escherichia coli were investigated. p-Aminobenzamidine prevented the solubilization of the Mg-ATPase during treatment of membranes with low-ionic-strength buffers containing ethylenediaminetetraacetic acid. p-Aminobenzamidine did not prevent subsequent solubilization of the Mg-ATPase by treatment of the membranes with chloroform. This method of solubilization yielded a preparation of similar apparent molecular weight but with a 10-fold-increased specific activity as compared with the Mg-ATPase solubilized by washing with low-ionic-strength buffer. However, in contrast to the latter preparation, the chloroform-solubilized Mg-ATPase did not reconstitute ATP-dependent energization of stripped membranes, which were prepared by low-ionic-strength washing in the absence of p-aminobenzamidine. Another protease inhibitor, epsilon-amino-n-caproic acid, did not effect the solubilization of the Mg-ATPase, but did inhibit the loss of activity occurring during concentration, by ultrafiltration, of the Mg-ATPase solublized by the low-ionic-strength treatment.

This article has been cited by other articles:

• Motz, C., Hornung, T., Kersten, M., McLachlin, D. T., Dunn, S. D., Wise, J. G., Vogel, P. D. (2004). The Subunit b Dimer of the FoF1-ATP Synthase: INTERACTION WITH F1-ATPase AS DEDUCED BY SITE-SPECIFIC SPIN-LABELING. J. Biol. Chem. 279: 49074-49081 [Abstract] [Full Text]  
• Pedersen, P. L., Hullihen, J., Bianchet, M., Amzel, L. M., Lebowitz, M. S. (1995). Rat Liver ATP Synthase. J. Biol. Chem. 270: 1775-1784 [Abstract] [Full Text]