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Journal ArticleDOI

Studies of sodium-potassium activated adenosine triphosphatase. vii. inhibitation by erythrophleum alkaloids.

TLDR
The similarity of the effects of the erythrophleine and cassaine alkaloids and the digitalis glycosides on the Na-K ATPase system may explain the remarkable similarity between these two groups of compounds in pharmacological properties and in inhibitory effects on active cation transport.
About
This article is published in Biochemical Pharmacology.The article was published on 1964-01-01. It has received 57 citations till now. The article focuses on the topics: ATPase & Ouabain.

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Citations
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Journal ArticleDOI

The sodium-potassium adenosinetriphosphatase.

Dahl Jl, +1 more
TL;DR: The Phosphorylated Peptide Component of Purified NaK A TPase Preparations and the Reversal of the Reaction are presented, which show the importance of knowing the carrier and removal status of the carrier molecule.
Book ChapterDOI

[116] Sodium and potassium-stimulated ATPase

R.L. Post, +1 more
TL;DR: The method is described that separates phosphomolybdate from ATP by extraction into butyl acetate and the general principle of purification procedure is to obtain a microsomal fraction by differential centrifugation of a sucrose homogenate and to form dispersed and activated particles with a detergent, urea, or a concentrated iodide solution.
Journal ArticleDOI

Studies on (Na+-K+)-activated ATPase. XXIV. Localization and properties of ATPase in the inner ear of the guinea pig.

TL;DR: The results strongly suggest that the (Na+-K+)-ATPase system in the stria vascularis plays the primary role in the maintenance of the cochlear cation gradients, while the contribution of Reissner's membrane to this process can only be very minor.
Journal ArticleDOI

Physiologic Role of Sodium-Potassium-Activated Adenosine Triphosphatase in the Transport of Cations across Biologic Membranes

TL;DR: The chiral stationary phase of Na-K-ATPase acts as a “spatially aggregating force” to knock out the “bad guys” in the EMTs.
Journal ArticleDOI

Studies on sodium-potassium-activated adenosinetriphosphatase. xi. the salt gland of the herring gull.

TL;DR: The high molar activity of carbonic anhydrase, which was not significantly changed in the fresh water animals, indicates that this enzyme can only play a secondary nonlimiting role in the salt secretion process.
References
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Journal ArticleDOI

The influence of some cations on an adenosine triphosphatase from peripheral nerves.

TL;DR: Leg nerves from the shore crab contain an adenosine triphosphatase which is located in the submicroscopic particles, and the influence of sodium, potassium, magnesium and calcium ions on this enzyme has been investigated.
Journal ArticleDOI

The influence of some cations on an adenosine triphosphatase from peripheral nerves.

TL;DR: In this article, the authors investigated the influence of different cations on the activity of an adenosine triphosphatase (ATP) enzyme in the leg nerves of crabs.
Journal ArticleDOI

Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte.

TL;DR: Evidence is presented that an adenosine triphosphatase in broken human erythrocyte membranes is a part of the system for the active transport of sodium and potassium in intact ery Throthrocytes.
Journal ArticleDOI

Further investigations on a Mg++ + Na+-activated adenosintriphosphatase, possibly related to the active, linked transport of Na+ and K+ across the nerve membrane

TL;DR: The observations lend further support to the suggestion made previously that this enzyme is involved in the active, linked transport of Na+ and K+ across the nerve membrane.
Journal ArticleDOI

Studies on sodium-potassium-activated adenosine triphosphatase: I. Quantitative distribution in several tissues of the cat

TL;DR: The quantitative distribution of sodium-potassium-activated adenosine triphosphatase, which had been shown to play a role in active transport of sodium and potassium in erythrocytes, has been determined in 36 tissues of the cat and in human retina, ciliary body, and ery Throcytes.
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