Literature DB >> 6259330

Excess magnesium converts red cell (sodium+potassium) ATPase to the potassium phosphatase.

P W Flatman, V L Lew.   

Abstract

1. The ATPase and phosphatase activities of red cell membranes were measured simultaneously as a function of the magnesium content of the medium. 2. It was found that when the magnesium concentration was greater than that of ATP, magnesium inhibited the ATPase and simultaneously stimulated the phosphatase. The concentrations of magnesium needed for half-maximal stimulation of the phosphatase and half-maximal inhibition of the ATPase were similar. 3. It is suggested that increasing the concentration of magnesium directly causes a change in the conformation of the enzyme from one which favours ATPase activity to one which favours phosphatase activity.

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Year:  1980        PMID: 6259330      PMCID: PMC1283029          DOI: 10.1113/jphysiol.1980.sp013419

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  15 in total

1.  Effect of ATP on the intermediary steps of the reaction of the (Na+ plus K+)-dependent enzyme system. 3. Effect on the p-nitrophenylphosphatase activity of the system.

Authors:  J C Skou
Journal:  Biochim Biophys Acta       Date:  1974-03-15

2.  Nucleotide and divalent cation interactions with the (Na+ plus K+)-dependent ATPase.

Authors:  J D Robinson
Journal:  Biochim Biophys Acta       Date:  1974-03-21

3.  Purification and characterization of (Na+ + K+)-ATPase. II. Preparation by zonal centrifugation of highly active (Na+ + K+)-ATPase from the outer medulla of rabbit kidneys.

Authors:  P L Jorgensen; J C Skou; L P Solomonson
Journal:  Biochim Biophys Acta       Date:  1971-04-13

4.  Potassium activated phosphatase from human red blood cells. The mechanism of potassium activation.

Authors:  P J Garrahan; M I Pouchan; A F Rega
Journal:  J Physiol       Date:  1969-06       Impact factor: 5.182

5.  Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase.

Authors:  R L Post; C Hegyvary; S Kume
Journal:  J Biol Chem       Date:  1972-10-25       Impact factor: 5.157

6.  Kinetic studies on a brain microsomal adenosine triphosphatase. II. Potassium-dependent phosphatase activity.

Authors:  J D Robinson
Journal:  Biochemistry       Date:  1969-08       Impact factor: 3.162

7.  A cycle for ouabain inhibition of sodium- and potassium-dependent adenosine triphosphatase.

Authors:  A K Sen; T Tobin
Journal:  J Biol Chem       Date:  1969-12-25       Impact factor: 5.157

8.  Kinetic studies of membrane (Na+-K+-Mg2+)-ATPase.

Authors:  T Hexum; F E Samson; R H Himes
Journal:  Biochim Biophys Acta       Date:  1970-08-15

9.  Interaction of haemoglobin with ions. Interactions among magnesium, adenosine 5'-triphosphate, 2,3-bisphosphoglycerate, and oxygenated and deoxygenated human haemoglobin under simulated intracellular conditions.

Authors:  H Berger; G R Jänig; G Gerber; K Ruckpaul; S M Rapoport
Journal:  Eur J Biochem       Date:  1973-10-18

10.  Synthesis of adenosine triphosphate by way of potassium-sensitive phosphoenzyme of sodium, potassium adenosine triphosphatase.

Authors:  R L Post; G Toda; S Kume; K Taniguchi
Journal:  J Supramol Struct       Date:  1975
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  4 in total

1.  Effects of deoxygenation on active and passive Ca2+ transport and on the cytoplasmic Ca2+ levels of sickle cell anemia red cells.

Authors:  Z Etzion; T Tiffert; R M Bookchin; V L Lew
Journal:  J Clin Invest       Date:  1993-11       Impact factor: 14.808

2.  Deoxygenation permeabilizes sickle cell anaemia red cells to magnesium and reverses its gradient in the dense cells.

Authors:  O E Ortiz; V L Lew; R M Bookchin
Journal:  J Physiol       Date:  1990-08       Impact factor: 5.182

3.  Interaction of magnesium with the sodium pump of the human red cell.

Authors:  J R Sachs
Journal:  J Physiol       Date:  1988-06       Impact factor: 5.182

4.  The magnesium dependence of sodium-pump-mediated sodium-potassium and sodium-sodium exchange in intact human red cells.

Authors:  P W Flatman; V L Lew
Journal:  J Physiol       Date:  1981-06       Impact factor: 5.182

  4 in total

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