Search Results - "Karlish, S.J.D."

General and specific lipid–protein interactions in Na,K-ATPase by Cornelius, F., Habeck, M., Kanai, R., Toyoshima, C., Karlish, S.J.D.

“…The molecular activity of Na,K-ATPase and other P2 ATPases like Ca2+-ATPase is influenced by the lipid environment via both general (physical) and specific…”
Get full text

Tryptophan fluorescence of (Na+ + K+)-ATPase as a tool for study of the enzyme mechanism by Karlish, S J, Yates, D W

“…1. The protein fluorescence intensity of (Na+ + K+)-ATPase is enhanced following binding of K+ at low concentrations. The properties of the response suggest…”
Get more information

Specific Cu2+ -catalyzed oxidative cleavage of Na,K-ATPase at the extracellular surface by Shimon, M.B. (Weizmann Institute of Science, Rehovot, Israel.), Goldshleger, R, Karlish, S.J.D

“…This paper describes specific Cu 2+ -catalyzed oxidative cleavage of α and β subunits of Na,K-ATPase at the extracellular surface. Incubation of right…”
Get full text

Dinitrophenol and valinomycin as uncouplers in isolated chloroplasts by Karlish, S.J.D., Avron, M.

Get full text

Characterization of disulfide cross-links between fragments of proteolyzed Na,K-ATPase. Implications for spatial organization of trans-membrane helices by Or, E. (University of Basel, Switzerland.), Goldshleger, R, Karlish, S.J.D

“…This study characterizes disulfide cross-links between fragments of a well defined tryptic preparation of Na,K-ATPase, 19-kDa membranes solubilized with C12E10…”
Get full text

A 19-kDA C-Terminal Tryptic Fragment of the α Chain of Na/K-ATPase is Essential for Occlusion and Transport of Cations by Karlish, S. J. D., Goldshleger, R., Stein, W. D.

“…Tryptic digestion of pig renal Na/K-ATPase in the presence of Rb and absence of Ca ions removes about half of the protein but leaves a stable 19-kDa…”
Get full text

Identification of the loop region between TM5 and TM6 of the H,K ATPase using cysteine mutagenesis by Lambrecht, N., Corbett, Z., Bayle, D., Karlish, S.J.D., Sachs, G.

Get full text

Evidence That Ser775 in the α Subunit of the Na,K-ATPase Is a Residue in the Cation Binding Pocket by Blostein, Rhoda, Wilczynska, Ania, Karlish, Steven J.D., Argüello, Jose M., Lingrel, Jerry B

“…Substitution of alanine for Ser775 in a ouabain-resistant α1 sheep isoform causes a 30-fold decrease in apparent affinity for K+ as an activator of the…”
Get full text

Use of formycin nucleotides, intrinsic protein fluorescence, and fluorescein isothiocyanate-labeled enzymes for measurement of conformational states of Na+,K+-ATPase by Karlish, S J

Get more information

Regulatory interaction between calmodulin and ATP on the red cell Ca2+ pump by Muallem, S, Karlish, S J

“…The interactions between calmodulin, ATP and Ca2+ on the red cell Ca2+ pump have been studied in membranes stripped of native calmodulin or rebound with…”
Get more information

Identification and reconstitution of a Na+/K+/Cl- cotransporter and K+ channel from luminal membranes of renal red outer medulla by Burnham, C, Karlish, S J, Jørgensen, P L

“…Electrophysiological studies on renal thick ascending limb segments indicate the involvement of a luminal Na+/K+/Cl- cotransport system and a K+ channel in…”
Get more information

Transport studies by optical methods by Sachs, G, Rabon, E, Karlish, S J

Get more information

Evidence for the presence of 'ouabain like' compound in human cerebrospinal fluid by Lichtstein, D, Minc, D, Bourrit, A, Deutsch, J, Karlish, S J, Belmaker, H, Rimon, R, Palo, J

“…Material extracted and partially purified from human cerebrospinal fluid (CSF) is capable of: a, inhibiting [3H]ouabain binding to rat brain synaptosomes; b,…”
Get more information

A simple, rapid and efficient procedure for purification of calmodulin from human red cells by Muallem, S., Karlish, S.J.D.

Get full text

Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotides by Karlish, S J, Yates, D W, Glynn, I M

“…1. Fluorescence measurements have shown that formycin triphosphate (FTP) or formycin diphosphate (FDP) bound to (Na+ + K+)-ATPase (ATP phosphohydrolase, EC…”
Get more information

Kinetic parameters of glucose efflux from human red blood cells under zero-trans conditions by Karlish, S J, Lieb, W R, Ram, D, Stein, W D

Get more information

Elementary steps of the (Na+ + K+)-ATPase mechanism, studied with formycin nucleotides by Karlish, S J, Yates, D W, Glynn, I M

“…1. Formycin triphosphate (FTP), a fluorescent analogue of ATP, is a substrate for (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3), with properties similar…”
Get more information