Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Inhibition, by a protease inhibitor, of the solubilization of the F1-portion of the Mg2+-stimulated adenosine triphosphatase of Escherichia coli. 14 33

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).
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PMID:Solubilization of adenosine triphosphatase from membranes of Escherichia coli: effect of p-aminobenzamidine. 15 91

Ammopiptanthus mongolicus is the only evergreen broadleaf shrub endemic to the Alashan desert, northwest sand area of China, and can survive -30 degrees C or an even lower temperature in winter. A modified solid-phase subtraction hybridization technique was developed to isolate and screen cDNAs whose transcripts increased in cold-treated A. mongolicus seedlings. Sequence analysis of the screened clones indicated that 11 clones had coding regions, with four of them containing a complete open reading frame. Nine of the 11 clones shared various degrees of homology with the genes found in the GenBank database and the other two were unidentified sequences. Sequence data further revealed that these accumulated transcripts encoded: three low molecular weight proteins (a late-embryogenesis protein and two cold acclimation responsive proteins); two photosynthesis-related proteins, (photosystem I subunit II precursor (PsaD) and photosystem II oxygen-evolving complex 33kDa subunit OEC33); a protease inhibitor; an adenosine triphosphatase and a 14-3-3 related protein. Analysis of the function of these proteins indicated that the low molecular weight proteins were associated with water holding ability of cytoplasm, photosynthesis-related proteins participated in the adjustments of photosynthetic apparatus to resist photoinhibition; 14-3-3 related protein could interact with adenosine triphosphatase to enhance ATPase activity and energy metabolism, and protease inhibitor is involved in the prevention of unwanted cell death caused by reactive oxygen species. We suggest that cold acclimation with low light intensity in A. mongolicus is a more complex interaction of low temperature, light, energy and signal than that assumed previously.
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PMID:Functional analysis of cold-inducible cDNA clones in the legume Ammopiptanthus mongolicus. 1982 50