Literature DB >> 6224706

Is Ca2+-ATPase a water pump?

Y Dupont.   

Abstract

The mechanism of free energy coupling in active transport is discussed with special reference to the sarcoplasmic reticulum Ca2+-ATPase. In the current working schemes for cation transport ATPases, free energy transduction is nearly always based on enzyme conformational changes. The principal objective of the present article is to examine whether recent experimental results on Ca2+-ATPase may in fact be better explained by assuming the existence of a direct chemiosmotic process. In the scheme proposed, free energy transduction between ATP and calcium is based on a transfer of solvation water between the acylphosphate bond and the bound calcium ions.

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Year:  1983        PMID: 6224706     DOI: 10.1016/0014-5793(83)80721-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Cytochemical localization of ouabain-sensitive, K+ -dependent p-nitrophenylphosphatase and Ca++-stimulated adenosine triphosphatase activities in human parotid and submandibular glands.

Authors:  M Cossu; M S Lantini; P Puxeddu; A Riva
Journal:  Histochemistry       Date:  1984

2.  Function of the N-acetyl-L-histidine system in the vertebrate eye. Evidence in support of a role as a molecular water pump.

Authors:  M H Baslow
Journal:  J Mol Neurosci       Date:  1998-06       Impact factor: 3.444

  2 in total

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