Literature DB >> 6272854

Radiation inactivation of (Na+ + K+)-ATPase. A small target size for the K+-occluding mechanism.

D E Richards, J C Ellory, I M Glynn.   

Abstract

Radiation inactivation of partially purified (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) from pig kidney outer medulla shows that the target size for Rb+ occlusion by the enzyme (in the absence of phosphorylation) is much smaller than the target size for p-nitrophenyl phosphatase activity, which is itself smaller than the reported target size for (Na+ + K+)-ATPase activity.

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Year:  1981        PMID: 6272854     DOI: 10.1016/0005-2736(81)90045-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  K+-stimulated p-nitrophenyl phosphatase is not a partial reaction of the gastric (H+ + K+)-transporting ATPase. Evidence supporting a new model for the univalent-cation-transporting ATPase systems.

Authors:  T K Ray; J Nandi
Journal:  Biochem J       Date:  1986-01-01       Impact factor: 3.857

Review 2.  Annual review prize lecture. 'All hands to the sodium pump'.

Authors:  I M Glynn
Journal:  J Physiol       Date:  1993-03       Impact factor: 5.182

3.  Occlusion of rubidium ions by the sodium-potassium pump: its implications for the mechanism of potassium transport.

Authors:  I M Glynn; D E Richards
Journal:  J Physiol       Date:  1982-09       Impact factor: 5.182

  3 in total

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