Ca2+ Fluxes and Regulation: E. Carafoli, Membrane Transport of Calcium: An Overview. A. Complex Systems and Subcellular Fractions Involved in Ca2+ Regulation: M. Endo and M. Lino, Measurement of Ca2+ Release in Skinned Fibers from Skeletal Muscle. S. Seiler and S. Fleischer, Isolation and Characterization of Sarcolemmal Vesicles from Rabbit Fast Skeletal Muscle. A. Chu, M.C. Dixon, A. Saito, S. Seiler, and S. Fleischer, Isolation of Sarcoplasmic Reticulum Fractions Referable to Longitudinal Tubules and Junctional Terminal Cisternae from Rabbit Skeletal Muscle. B. Costello, C. Chadwick, and S. Fleischer, Isolation of the Junctional Face Membrane of Sarcoplasmic Reticulum. R.D. Mitchell, P. Palade, A. Saito, and S. Fleischer, Isolation of Triads from Skeletal Muscle. A.H. Caswell, N.R. Brandt, J.R. Brunschwig, and R.M. Kawamoto, Isolation of Transverse Tubule Membranes from Skeletal Muscle: Ion Transport Activity, Reformation of Triad Junctions, and Isolation of Junctional Spanning Protein of Triads. L.R. Jones, Rapid Preparation of Canine Cardiac Sarcolemmal Vesicles by Sucrose Flotation. B.K. Chamberlain and S. Fleischer, Isolation of Canine Cardiac Sarcoplasmic Reticulum. M. Inui, S. Wang, A. Saito, and S. Fleischer, Junctional and Longitudinal Sarcoplasmic Reticulum of Heart Muscle. M. Tada, M. Kadoma, M. Inui, and J. Fujii, Regulation of Ca2+-Pump from Cardiac Sarcoplasmic Reticulum. B. Characterization of Ca2+-Pumps and Modulators from Various Sources: G. Inesi, M. Kurzmack, and D. Lewis, Kinetic and Equilibrium Characterization of an Energy-Transducing Enzyme and Its Partial Reactions. L. de Meis, Approaches to Studying the Mechanisms of ATP Synthesis in Sarcoplasmic Reticulum. Y. Dupont, F. Guillain, and J.J. Lacapere, Fluorimetric Detection and Significance of Conformational Changes in Ca2+-ATPase. E. Fassold and W. Hasselbach, Synthesis of ATP From Ca2+ Gradient by Sarcoplasmic Reticulum Ca2+-Transport ATPase. H. Takisawa and M. Makinose, Occluded Ca2+. M. Yamaguchi and T. Watanabe, Modified Membrane Filtration Methods for Ligand Binding on ATP-Driven Pumps during ATP Hydrolysis. T.Y. Tsong, Active Cation Pumping of Na+, K+-ATPase and Sarcoplasmic Reticulum Ca2+-ATPase Induced by an Electric Field. M. Kawakita, K. Yasuoka-Yabe, K. Saito-Nakatsuka, A. Baba, and T. Yamashita, Chemical Derivatization of Ca2+-Pump Protein from Skeletal Muscle with N-Substituted Maleimides and 5-(2-Iodoacetamidoethyl)aminonaphthalene- 1-Sulfonate. J.V. M~aloller, M. le Maire, and J.P. Andersen, Use of Detergents to Solubilize the Ca2+-Pump Protein as Monomers and Defined Oligomers. K.A. Taylor, L. Dux, S. Varga, H.P. Ting-Beall, and A. Martonosi, Analysis of Two-Dimensional Crystals of Ca2+-ATPase in Sarcoplasmic Reticulum. C.J. Brandi, L. Fliegel, and D.H. Mac Lennan, cDNA Cloning of Sarcoplasmic Reticulum Proteins. L. Hymel and S. Fleischer, Reconstitution of Skeletal Muscle Sarcoplasmic Reticulum Membranes: Strategies for Varying the Lipid/Protein Ratio. M. Inui and S. Fleischer, Reconstitution of Calcium Pumping of Cardiac Sarcoplasmic Reticulum. A. Maurer, M. Tanaka, T. Ozawa, and S. Fleischer, Purification and Crystallization of Calcium-Binding Protein from Skeletal Muscle Sarcoplasmic Reticulum. T.J. Lukas and D.M. Watterson, Purification of Calmodulin and Preparation of Immobilized Calmodulin. J.T. Penniston, A.G. Filoteo, C.S. McDonough, and E. Carafoli, Purification, Reconstitution, and Regulation of Plasma Membrane Ca2+-Pumps. W.L. Dean, Isolation and Reconstitution of Ca2+-Pump from Human and Porcine Platelets. L.R. Jones, A.D. Wegener, and H.K.B. Simmerman, Purification of Phospholamban from Canine Cardiac Sarcoplasmic Reticulum Vesicles by Use of Sulfhydryl Group Affinity Chromatography. J. Lunardi, P. De Foor, and S. Fleischer, Modification of Phospholipid Environment in Sarcoplasmic Reticulum Using Nonspecific Phospholipid Transfer Protein. C. Ca2+ and Other Channels: A. Fabiato, Computer Programs for Calculating Total from Specified Free or Free from Specified Total Ionic Concentrations in Aqueous Solutions Containing Multiple Metals and Ligands. G. Meissner, Ionic Permeability of Isolated Muscle Sarcoplasmic Reticulum and Liver Endoplasmic Reticulum Vesicles. M. Kasai and K. Nunogaki, Permeability of Sarcoplasmic Reticulum. N. Ikemoto, D.H. Kim, and B. Antoniu, Measurement of Calcium Release in Isolated Membrane Systems: Coupling between the Transverse-Tubule and Sarcoplasmic Reticulum. J.S. Smith, R. Coronado, and G. Meissner, Techniques for Observing Calcium Channels from Skeletal Muscle Sarcoplasmic Reticulum in Planar Lipid Bilayers. M. Inui and S. Fleischer, Purification of Ryanodine Receptor from Sarcoplasmic Reticulum. J.P. Reeves, Measurement of Sodium-Calcium Exchange Activity in Plasma Membrane Vesicles. ATP-Driven Proton Pumps. J.-P. Dufour, A. Armory, and A. Goffeau, Plasma Membrane ATPase from the Yeast Schizosaccharomyces pombe. A. Goffeau and J.-P. Dufour, Plasma Membrane ATPase from the Yeast Saccharomyces Cerevisiae. R. Serrano, H+-ATPase from Plasma Membranes of Saccharomyces cerevisiae and Avena sativa roots: Purification and Reconstitution. E. Uchida, Y. Ohsumi, and Y. Anraku, Purification of Yeast Vacuolar Membrane H+-ATPase and Enzymological Discrimination of Three ATP-Driven Proton Pumps in Saccharomyces cerevisiae. E.J. Bowman and B.J. Bowman, Purification of Vacuolar Membranes, Mitochondria, and Plasma Membranes from Neurospora crassa and Modes of Discrimination among the Different H+-ATPases. G.A. Scarborough, Large-Scale Purification of Plasma Membrane H+-ATPase from a Cell Wall-less Mutant of Neurospora crassa. A.B. Bennett, R.A. Leigh, and R.M. Spanswick, H+-ATPase from Vacuolar Membranes of Higher Plants. D.L. Schneider and J. Chin, Preparation and Acidification Activity of Lysosomes and Lysosomal Membranes. C.J. Galloway, G.E. Dean, R. Fuchs, and I. Mellman, Analysis of Endosome and Lysosome Acidification in Vitro. A. Lowe and Q. Al-Awqati, Proton ATPases in Golgi Vesicles and Endoplasmic Reticulum: Characterization and Reconstitution of Proton Pumping. N. Nelson, S. Cidon, and Y. Moriyama, Chromaffin Granule Proton Pump. X.-S. Xie, D.K. Stone, and E. Racker, Proton Pump of Clathrin-Coated Vesicles. ATP-Driven K+ Pumps. E.C. Rabon, W.B. Im, and G. Sachs, Preparation of Gastric H+K+-ATPase. J.L.W. Polarek, M.O. Walderhaug, and W. Epstein, Genetics of Kpd, the K+-Transport ATPase of E. coli. A. Siebers, L. Wieczorek, and K. Altendorf, K+-ATPase from Escherichia coli: Isolation and Characterization. M. Solioz and P. Furst, Purification of K+ATPase of Streptoccocus faecalis. Author Index. Subject Index.
The transport volumes of the Biomembranes series were initiated with Volumes 125 and 126 of Methods in Enzymology. These two volumes covered Transport in Bacteria, Mitochondria, and Chloroplasts. Volumes 156 and 157 cover ATP-Driven Pumps and Related Transport. The topic of biological membrane transport is a very timely one because a strong conceptual basis for its understanding now exists.
Biochemists, cell biologists, microbiologists, pharmacologists, biomedical scientists, biophysicists, analytical chemists, and physiologists.
- No. of pages:
- © Academic Press 1988
- 28th October 1988
- Academic Press
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Vanderbilt University, Nashville, Tennessee, U.S.A.
Vanderbilt University, Nashville, Tennesse, U.S.A.
Elsevier.com visitor survey
We are always looking for ways to improve customer experience on Elsevier.com.
We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit.
If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website.
Thanks in advance for your time.