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- W997556594 abstract "The presence of an active Na+, K+-ATPase in the same tissue that has been employed widely to study organic solute transport—regardless of localization—is highly important because the enzymatic mechanism for maintaining low intracellular concentration of sodium would, of course, be required to establish any proposal for sodium-dependent solute transport. The chapter discusses (1) the possible role of the Na+, K+-ATPase enzyme system in amino acid transport, (2) the possible relationship between the Na+, K+-ATPase and sugar transport, and (3) some complications of sugar transport in relation to the Na+, K+-ATPase. If the Na+, K +-ATPase enzyme system, and/or if a sodium pump, in some way, is involved in the transport of amino acids and other organic solutes, the specific inhibitor of the pump, ouabain, or any active cardiotonic glycoside, should produce some effect on the solute transport. To examine the possible role of the Na+, K+-ATPase enzyme system, epithelium-like cells and aneuploid cells originally isolated from human carcinoma of the oral cavity was employed and advantage was taken of interesting observations concerning impairment of the transport of α-aminoisobutyric acid (AIB) by inositol deprivation. The experiments were designed to provide information on whether inositol deprivation impairs exchange fluxes in addition to its inhibitory effect on transport fluxes. It should also be emphasized, however, that sodium-dependent amino acid transport in some tissues appears to be insensitive to ouabain at concentrations that normally cause significant inhibition of the Na+, K+-pump as well as of the Na+ , K+-ATPase." @default.
- W997556594 created "2016-06-24" @default.
- W997556594 creator A5038785455 @default.
- W997556594 creator A5065363939 @default.
- W997556594 creator A5073170005 @default.
- W997556594 date "1972-01-01" @default.
- W997556594 modified "2023-10-16" @default.
- W997556594 title "The Na+, K+-ATPase Membrane Transport System: Importance in Cellular Function" @default.
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