Biomembranes Part P: ATP-Driven Pumps and Related Transport: by Sidney Fleischer, Becca Fleischer

By Sidney Fleischer, Becca Fleischer

The severely acclaimed laboratory normal, Methods in Enzymology, is without doubt one of the so much hugely revered guides within the box of biochemistry. due to the fact 1955, each one quantity has been eagerly awaited, often consulted, and praised via researchers and reviewers alike. The sequence includes a lot fabric nonetheless proper at the present time - really a vital booklet for researchers in all fields of existence sciences

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Extra resources for Biomembranes Part P: ATP-Driven Pumps and Related Transport: The Na,K-Pump

Sample text

Based on kinetic experiments (see Refs. 6 and 7) and 76 T. J. B. Simmons, J. Physiol. (London) 244, 731 (1975). 77 S. P. Banerjee and S. M. E. Wong, J. Biol. Chem. 247, 5409 (1972). 7s j. D. Robinson, Biochim. Biophys. Acta 484, 161 (1977). [1] OVERVIEW: THE Na,K-PUMP 25 from the effect of Li + on the phosphatase activity, 35it has been postulated that there are simultaneously existing extracellular and cytoplasmic sites and that the reaction, which leads to the N a + - K + exchange, occurs with simultaneous binding of K + to the extracellular sites and of Na ÷ to the cytoplasmic sites.

H H. Hebert, P. 'JCrgensen, E. Skriver, and A. B. Maunsbach, Biochim. Biophys. Acta 689, 571 (1982). i2 p. L. JCrgensen, Biochim. Biophys. Acta 694, 27 (1982). 13 p. L. JCrgensen, E. Skriver, H. Hebert, and A. B. Maunsbach, Ann. N. Y. Acad. Sci. 402, 207 (1982). METHODS IN ENZYMOLOGY,VOL. 156 Copyright© 1988by AcademicPress. Inc. All rightsof reproductionin any formreserved. 30 PREPARATION OF N a + , K + - A T P a s e AND SUBUNITS [2] of molecular weight by analytical ultracentrifugation and gel chromatography.

However, Vmaxfor the Na ÷ + K+-dependent hydrolysis of ATP decreases in proportion to the number of ouabain molecules prebound. This shows that ouabain bound to one a,fl has no effect on Vm~ for the hydrolytic activity of another a,fl, and suggests no cooperativity between two a,fl units for hydrolysis. This agrees with the observation that a,/3 obtained by detergent dissociation of (a, 13)2has Na ÷ + K+-dependent ATPase activity. Thus, under certain conditions there is interaction between binding sites on different a,fl units which have Na+,K+-ATPase activity, but apparently there is no interaction between the units for the Na+,K+-ATPase activity.

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