Biomembranes: Biomembranes, Part P: ATP-Driven Pumps and Related Transport: The Na,K-Pump ATP-Driven Pumps and Related Transport: the Na,K-Pump: Part P Volume 156

Biomembranes: Biomembranes, Part P: ATP-Driven Pumps and Related Transport: The Na,K-Pump ATP-Driven Pumps and Related Transport: the Na,K-Pump: Part P Volume 156

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The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.
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Product details

  • Hardback | 468 pages
  • 152.4 x 231.1 x 27.9mm | 839.16g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 0121820572
  • 9780121820572

Table of contents

J.C. Skou, Overview: The Na,K-Pump. Preparation of Na+,K+-ATPase and Subunits. P.L. Jorgensen, Purification of Na+,K+-ATPase: Enzyme Sources, Preparative Problems, and Preparation from Mammalian Kidney. J.C. Skou and M. Esmann, Preparation of Membrane Na+,K+-ATPase from Rectal Glands of Squalus acanthias. T.W. Smith, Purification of Na+,K+-ATPase from the Supraorbital Salt Gland of the Duck. G.L. Peterson and L.E. Hokin, Preparation of Na+,K+-ATPase from Brine Shrimp. K.J. Sweadner, Preparation of the *ga(+) Isozyme of the Na+,K+-ATPase from Mammalian Axolemma. M. Esmann, Solubilization of Na+,K+-ATPase. E. Skriver, A.B. Maunsbach, H. Hebert, and P.L. Jorgensen, Crystallization of Membrane-Bound Na+,K+-ATPase in Two Dimensions. W.J. Ball, Jr., T.L. Kirley, and L.K. Lane, Preparation of Antibodies to Na+,K+-ATPase and Its Subunits. Assay of Na+,K+-ATPase Activity. M. Esmann, ATPase and Phosphatase Activity of Na+,K+-ATPase: Molar and Specific Activity, Protein Determination. J.G. Norby, Coupled Assay of Na+,K+-ATPase Activity. M.D. Resh, Identification and Quantitation of Na+,K+-ATPase by Back-Door Phosphorylation. Reconstitution of Na,K-Pump Activity. S.M. Goldin, M. Forgac, and G. Chin, Reconstitution of Na,K-Pump Activity by Cholate Dialysis: Sidedness and Stoichiometry. L.E. Hokin and J.F. Dixon, Reconstitution of the Na,K-Pump by Freeze*b1Thaw Sonication: Estimation of Coupling Ratio and Electrogenicity. F. Cornelius, Incorporation of C12E8-Solubilized Na+,K+-ATPase into Liposomes: Determination of Sidedness and Orientation. Analysis of the Pump Cycle. R. Blostein, Measurement of Na+ and K+ Transport and Na+,K+-ATPase Activity in Inside-Out Vesicles from Mammalian Erythrocytes. S.J.D. Karlish, Measurement of Active and Passive Na+ and K+ Fluxes in Reconstituted Vesicles. Measurement of Ligand Binding and Distance between Ligands. J.G. Norby and J. Jensen, Measurement of Binding of ATP and ADP to Na+,K+-ATPase. E.T. Wallick and A. Schwartz, Interaction of Cardiac Glycosides with Na+,K+-ATPase. S.R. Hootman and S.A. Ernst, Estimation of Na,K-Pump Numbers and Turnover in Intact Cells with [3H]Ouabain. H. Matsui and H. Homareda, Measurement of Binding of Na+, K+, and Rb+ to Na+,K+-ATPase by Centrifugation Methods. J.D. Robinson, Estimating Affinities for Physiological Ligands and Inhibitors by Kinetic Studies on Na+,K+-ATPase and Its Partial Activities. L. Beaugi, Inhibition of Translocation Reactions by Vanadate. Measurements of Conformational States of Na+,K+-ATPase. S.J.D. Karlish, Use of Formycin Nucleotides, Intrinsic Protein Fluorescence, and Fluorescein Isothiocyanate-Labeled Enzymes for Measurement of Conformational States of Na+,K+-ATPase. J.C. Skou and M. Esmann, Eosin as a Fluorescence Probe for Measurement of Conformational States of Na+,K+-ATPase. I.M. Glynn, D.E. Richards, and L. Beaugi, Rapid Ion-Exchange Technique for Measuring Rates of Release of Occluded Ions. Modification of Na+,K+-ATPase. P.L. Jorgensen and R.A. Farley, Proteolytic Cleavage as a Tool for Studying Structure and Conformation of Pure Membrane-Bound Na+,K+-ATPase. W. Schoner, M. Hasselberg, and R. Kison, Irreversible and Reversible Modification of SH Groups and Effect on Catalytic Activity. W. Schoner and G. Scheiner-Bobis, Photoaffinity Labeling with ATP Analogs. B. Rossi and M. Lazdunski, Affinity Labeling of the Digitalis-Binding Site. W.S. Craig, Determination of Quaternary Structure of an Active Enzyme Using Chemical Cross-Linking with Glutaraldehyde. W.-h. Huang, S.S. Kakar, S.M. Periyasamy, and A. Askari, Use of Cross-Linking Reagents for Detection of Subunit Interactions of Membrane-Bound Na+,K+-ATPase. Magnetic Resonance Studies of Na+,K+-ATPase. C.M. Grisham, Nuclear Magnetic Resonance Investigations of Na+,K+-ATPase. M. Esmann, Electron Spin Resonance Investigations of Na+,K+-ATPase. Biogenesis and Membrane Assembly. J.W. Schneider, R.W. Mercer, E.J. Benz, Jr., and R. Levenson, Molecular Cloning of Na+,K+-ATPase *ga Subunit Gene Using Antibody Probes. M. Kashgarian and D. Biemesderfer, Preparation and Use of Monoclonal Antibodies to Na+,K+-ATPase. Microscopy of Na+,K+-ATPase. H. Mayahara and K. Ogawa, Histochemical Localization of Na+,K+-ATPase. A.B. Maunsbach, E. Skriver, and P.L. Jorgensen, Analysis of Na+,K+-ATPase by Electron Microscopy. Author Index. Subject Index.
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