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

By Sidney Fleischer, Becca Fleischer

The severely acclaimed laboratory typical, Methods in Enzymology, is without doubt one of the such a lot hugely revered courses within the box of biochemistry. for the reason that 1955, every one quantity has been eagerly awaited, usually consulted, and praised by means of researchers and reviewers alike. The sequence includes a lot fabric nonetheless appropriate at the present time - really a vital ebook for researchers in all fields of existence sciences

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Hoffman, Curr. Top. Membr. Transp. 19, 693 (1983). [1] OVERVIEW: THE Na,K-PUMP 23 3 Nao A EfP : A E~-p ~-~. : E"p. p I E'= ,'fATP E'~~P(Na3) {, E',. ATP A! K2 J -4 E;(K2) ATP E;'ATP (K 2) E~'ATP"K2 " ~ 2K, FiG. 4. Schemes for the uncoupled Na ÷ efflux (A) and for the K÷-K + exchange (B) based on the scheme in Fig. 2. 24 OVERVIEW: THE Na,K-PUMP [1] hydrolysis of ATP and ATP can be replaced by a nonhydrolyzable ATP analog. TM Comments In the scheme shown in Fig. 2, the enzyme has one binding site for ATP, which according to the ligand-binding experiments means an a,fl structure.

JCrgensen, E. Skriver, and A. B. Maunsbach, Biochim. Biophys. Acta 689, 571 (1982). 71~H. Hebert, E. Skriver, and A. B. Maunsbach, FEBS Lett. 187, 182 (1985). 71b y . A. Ovchinnikov, V. V. Demin, A. N. Barnakov, A. P. Kuzin, A. V. Lunev, N. N. Modyanov, and K. N. Dzhandzhugazyan, FEBS Lett. 190, 73 (1985). [1] OVERVIEW: THE Na,K-PUMP 17 transport, can be measured. Therefore, can purification of the catalytic activity be taken as an indication of purification of the transport molecule, or does purification lead to dissociation of the coupling between the two activities?

16 Determination of Optimum Concentration of SDS for the Incubation Since SDS has a low critical micelle concentration the bulk of detergent added to the medium will partition into the membrane and the weight ratio of SDS/membrane mass will determine the inactivation. The sigmoid-shaped inactivation curves in Fig. 4 indicate that several SDS molecules are involved in the inactivation of one unit of Na+,K+-ATPase. At the optimum concentration for the purification Na ÷,K÷-ATPase is inactivated to 85-90% of maximum activity.

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