Download e-book for iPad: Current Topics in Membranes and Transport, Vol. 3 by Felix Bronner, Arnost Kleinzeller (Eds.)

By Felix Bronner, Arnost Kleinzeller (Eds.)

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Extra info for Current Topics in Membranes and Transport, Vol. 3

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Sodium a t low potassium stimulated activity, but a t higher potassium concentrations it inhibited activity. ATP and ADP inhibited activity presumably by competing with the substrate (p-nitrophenol or acetyl phosphate) ; inorganic phosphate and calcium inhibited activity probably by product inhibition and competition with magnesium, respectively. I<+-Pase catalyzed the hydrolysis of PNPP, carbamyl phosphate, and acetyl phosphate. Bader and Sen (1966) compared the responses of Na*,I<+-ATPase and I<+-Pase to a number of ligands.

B. Mechanism of Energy Transduction One of the fundamental problems of molecular biology is how energy is transduced from adenosine triphosphate (ATP) to acceptor molecules. , conversion of glucose to glucose 6-phosphate). But the phosphorylation of ADP driven by electron transport and the dephosphorylation of ATP coupled to osmotic, mechanical, and electrical work are poorly understood, and are consequently the subjects of numerous investigations. , 1959,1960,1964; Whittam, 1958; Dunham, 1957).

Mechanism (a) is not plausible because of the inherently low monovalent cationic solubilities in hydrophobic environments. It is possible, theoretically, to limit even more the types of mechanisms which may be functional in the sodium pump. It appears unlikely, for example, that transport would be mediated through the transfer of cation to a carrier complex in the membrane matrix, followed by unrestricted diffusion of the complex between the opposite surfaces. Such a THE N a + , K+-ATPare MEMBRANE TRANSPORT SYSTEM 19 process would allow lateral diffusion of the complex.

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