Sodium-Potassium Dependent Adenosine Triphosphatase of Mammalian Reticulocytes and Mature Red Blood Cells

Adel A. Yunis; Grace K. Arimura

doi:10.3181/00379727-121-30770

Sodium-Potassium Dependent Adenosine Triphosphatase of Mammalian Reticulocytes and Mature Red Blood Cells

Adel A. Yunis, Grace K. Arimura

Medicine

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The level of Na-K-dependent ATPase was found to be considerably higher in reticulocytes than in mature erythrocytes. The fall in enzyme activity in the red cell upon maturation occurring concomitantly with loss of capacity to concentrate aminoacids lends support to the hypothesis that Na-K-dependent ATPase plays an important role in the active transport of aminoacids.

Original language	English (US)
Pages (from-to)	327-329
Number of pages	3
Journal	Proceedings of the Society for Experimental Biology and Medicine
Volume	121
Issue number	2
DOIs	https://doi.org/10.3181/00379727-121-30770
State	Published - Feb 1966

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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title = "Sodium-Potassium Dependent Adenosine Triphosphatase of Mammalian Reticulocytes and Mature Red Blood Cells",

abstract = "The level of Na-K-dependent ATPase was found to be considerably higher in reticulocytes than in mature erythrocytes. The fall in enzyme activity in the red cell upon maturation occurring concomitantly with loss of capacity to concentrate aminoacids lends support to the hypothesis that Na-K-dependent ATPase plays an important role in the active transport of aminoacids.",

author = "Yunis, {Adel A.} and Arimura, {Grace K.}",

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AB - The level of Na-K-dependent ATPase was found to be considerably higher in reticulocytes than in mature erythrocytes. The fall in enzyme activity in the red cell upon maturation occurring concomitantly with loss of capacity to concentrate aminoacids lends support to the hypothesis that Na-K-dependent ATPase plays an important role in the active transport of aminoacids.

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