Sodium- and potassium-dependent adenosine triphosphatase activity in a rat-kidney endoplasmic reticulum fraction

Landon, Erwin J.; Norris, John L.

doi:10.1016/0006-3002(63)91081-3

Cited by 88 publications

(26 citation statements)

References 24 publications

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“…Tliis material is generally thought to arise from fragments of endoplasmic reticulum and be membranous in nature (Hokin and Hokin, 1960;Palade and Siekevitz, 1956;Siekevitz and Palade, 1958;Hanzon and Toscbi, 1959;DeRobertis et al,. 1961;Landon and Norris. 1963).…”

Section: Specificity Towards Substratementioning

confidence: 99%

“…Although the most definitive results have been obtained using intact human erythrocytes (Glynn, 1961;Whittam, 1962) where it has been shown that enzyme activity can be stimulated only by K+ external to the cell and Na"*" internal to the cell, considerable evidence has been obtained from an examination of the ATPase of broken cell preparations (Jamefelt, 1962a;Skou, 1962;Aldridge, 1962;Landon, 1962;Landon and Norris, 1963).…”

Section: Introductionmentioning

confidence: 99%

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Studies of the Mechanism of Cation Transport

Charnock¹,

Post²

1963

Aust J Exp Biol Med

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SUMMARY.The distribution und activity of adenosine-triphosphatase in homogenates and subfractions of guinea pig kidney cortex has bt-en examined. A portion of the activity associated with particulate fractions could IH; furlhtr stimulated, in the presence of magnesium ions, by the combined addition of sodium and potassium ions but not by the addition of either cation alone or in combination with choline.Treatment of the heavy microsome subfraction with deoxycholate resulted in a large increase in the specific activity of this enzyme, which now re(|uired sodium and potassium ions in a ratio of 4 : 1 for over 85 p.c. of its total activity. Under such conditions of cation stimulation, optimum pH was found to be between 7-5 and 8-0, and the enzyme also exhibited considerable temperature dependence and was stable up to 55° C.The cardiac glycoside Ouabain completely inhibited that portion of enzyme activity stimulated by monovalent cittions but was without effect on the activity observed in the presence of niiiKnesium ions alone.The effect of other reagents and hormones on the cation stimulated adenosine-triphosphatase activity was also examined, with a discussion of the possible significance of this enzyme in active cation transport.INTRODUCTION.

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Section: Specificity Towards Substratementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Studies of the Mechanism of Cation Transport

Charnock¹,

Post²

1963

Aust J Exp Biol Med

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“…A role for Na-K-ATPase in the bulk transfer of ions across epithelial cell barriers, on the other hand, is not established and has been little explored. The kidney would seem an ideal organ to test the hypothesis that Na-K-ATPase is involved in the active transport of sodium, since the enzymatic activity of kidney cell membranes is high (2,3) and the chief work of the kidney is the active reabsorption of the sodium contained in the glomerular filtrate.…”

Section: Introductionmentioning

confidence: 99%

The Role of Sodium-Potassium—Activated Adenosine Triphosphatase in the Reabsorption of Sodium by the Kidney*

Katz¹,

Epstein²

1967

J. Clin. Invest.

241

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“…This fraction has heen well documented by others as arising from the endoplasmic reticulum of cells and being membranous in nature (Siekevitz and Palade, 1958;Hanzen and Toschi, 1959;deRobertis et al, 1962;Landon and Norris, 1963;Schwartz, 1963).…”

Section: Discussionmentioning

confidence: 71%

“…Enzyme activity was associated with a 'lieavA'" microsome fraction (35,000 X g) thought to arise from membranous fragments of the endoplasmic reticulum (Siekevitz and Palade, 1958;Hanzon and Toschi, 1959;deRobertis et al, 1962;Landon and Norris. 1963).…”

Section: Introductionmentioning

confidence: 99%

Studies of the Mechanism of Cation Transport

Charnock

1963

Aust J Exp Biol Med

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SUMMARY.Membrane-bound cation stimulated adenosine-triphosphatase is thought to be closely associated with active ion transport phenomena. As this enzyme system requires the combination of both sodium and potassium ions for full activation its mechanism of action has been investigated under these conditions. Using adenosine triphosphate labelled with P^ô nly in the terminal position as substrate for the reaction we have been able to show that ATP^2 is hydroiysed to adenosine diphosphate and radioactive orthophosphate via a phosphorylated intermediate. Sodium but not potassium ions are required for the formation of this intermediate and adenosine diphosphate; potassium ions are subsequently required for dephosphorylation of the intermediate complex with tlie release of P-''^ orthophosphate -that is, both sodium and potassium ions arc required for the turnover of the intermediate in a two step reaction.The cardiac glycoside ouabain (Strophanthin-G) is without effect upon the formation of this intermediate complex, but can completely inhibit the K+ -requiring dephosphorylation reaction. Preliminary experiments indicate that sodium ions are bound to the enzyme system during the phosphorylation reaction and are released when this complex is broken down. Solvent extraction procedures designed to remove phospholipid components did not decrease the specific activity of the phosphorylaled intenncdiate which suggests that it is phosphoprotein in nature.

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Sodium- and potassium-dependent adenosine triphosphatase activity in a rat-kidney endoplasmic reticulum fraction

Cited by 88 publications

References 24 publications

Studies of the Mechanism of Cation Transport

Studies of the Mechanism of Cation Transport

The Role of Sodium-Potassium—Activated Adenosine Triphosphatase in the Reabsorption of Sodium by the Kidney*

Studies of the Mechanism of Cation Transport

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