rubidium has been researched along with alpha-chymotrypsin in 13 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 10 (76.92) | 18.7374 |
| 1990's | 2 (15.38) | 18.2507 |
| 2000's | 1 (7.69) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Glynn, IM; Richards, DE | 1 |
| Goldschleger, R; Karlish, SJ; Shani, M | 1 |
| Jørgensen, PL; Petersen, J | 1 |
| Forsén, S; Lindman, B; Lindqvist, I; Zeppezauer, M | 1 |
| Borsa, J; Chapman, JD; Long, DG; Sargent, MD | 1 |
| Borsa, J; Chapman, JD; Copps, TP; Long, DG; Sargent, MD | 3 |
| Jørgensen, PL | 1 |
| Chin, G; Forgac, M | 1 |
| Karlish, SJ; Shainskaya, A | 1 |
| Goldshleger, R; Karlish, SJ | 1 |
| Apell, HJ; Karlish, SJ; Schneeberger, A; Shainskaya, A | 1 |
13 other study(ies) available for rubidium and alpha-chymotrypsin
| Article | Year |
|---|---|
Evidence for the ordered release of rubidium ions occluded within individual protomers of dog kidney Na+,K+-ATPase.
Topics: Animals; Chymotrypsin; Dogs; Fluorescein-5-isothiocyanate; Fluoresceins; Kidney; Phosphoric Acids; Rubidium; Sodium-Potassium-Exchanging ATPase; Thiocyanates | 1989 |
Rb+ occlusion in renal (Na+ + K+)-ATPase characterized with a simple manual assay.
Topics: Adenosine Triphosphate; Animals; Binding, Competitive; Cations, Monovalent; Chymotrypsin; Cold Temperature; Kidney; Kinetics; Phosphates; Phosphorylation; Rubidium; Rubidium Radioisotopes; Sodium; Sodium-Potassium-Exchanging ATPase; Swine | 1987 |
Chymotryptic cleavage of alpha-subunit in E1-forms of renal (Na+ + K+)-ATPase: effects on enzymatic properties, ligand binding and cation exchange.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Chymotrypsin; Kidney Medulla; Kinetics; Macromolecular Substances; Models, Chemical; Molecular Weight; Osmolar Concentration; Potassium Chloride; Rubidium; Sodium Chloride; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine; Trypsin | 1985 |
A 81Br nuclear magnetic resonance study of bromide ion binding to proteins in aqueous solution.
Topics: Alcohol Oxidoreductases; Animals; Binding Sites; Bromides; Bromine; Carbonic Anhydrases; Ceruloplasmin; Chemical Phenomena; Chemistry; Chlorine; Chymotrypsin; Fibrinolysin; Horses; Humans; Hydrogen-Ion Concentration; Liver; Magnetic Resonance Spectroscopy; Methods; Muramidase; Proteins; Radioisotopes; Rubidium; Serum Albumin; Temperature | 1969 |
Extraordinary effects of specific monovalent cations on activation of reovirus transcriptase by chymotrypsin in vitro.
Topics: Ammonia; Animals; Centrifugation, Density Gradient; Cesium; Chymotrypsin; DNA-Directed RNA Polymerases; Drug Antagonism; Drug Synergism; Enzyme Activation; Hot Temperature; L Cells; Lithium; Mice; Nucleotides; Phosphoric Monoester Hydrolases; Potassium; Reoviridae; Rubidium; Sodium; Spectrophotometry; Tritium | 1973 |
New intermediate subviral particles in the in vitro uncoating of reovirus virions by chymotrypsin.
Topics: Animals; Carbon Isotopes; Centrifugation, Density Gradient; Cesium; Chymotrypsin; DNA-Directed RNA Polymerases; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; L Cells; Lithium; Mice; Microscopy, Electron; Nucleoproteins; Peptides; Phosphoric Monoester Hydrolases; Potassium; Reoviridae; RNA, Viral; Rubidium; Sodium; Tritium; Uridine; Viral Proteins | 1973 |
Reovirus transcriptase activation in vitro: further studies on the facilitation phenomenon.
Topics: Animals; Cesium; Chymotrypsin; DNA-Directed RNA Polymerases; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Glycine max; Isoflurophate; Kinetics; L Cells; Mice; Potassium; Reoviridae; Rubidium; Sodium; Spectrophotometry, Atomic; Time Factors; Tosyl Compounds; Trypsin Inhibitors | 1974 |
Specific monovalent cation effects on modification of reovirus infectivity by chymotrypsin digestion in vitro.
Topics: Animals; Cesium; Chymotrypsin; DNA-Directed RNA Polymerases; Enzyme Activation; L Cells; Lithium; Mice; Potassium; Reoviridae; Rubidium; Sodium | 1973 |
Conformational changes in the alpha-subunit and cation transport by pure Na, K-ATPase.
Topics: Animals; Aspartic Acid; Biological Transport, Active; Chymotrypsin; Kinetics; Lipid Bilayers; Macromolecular Substances; Molecular Weight; Peptide Fragments; Phosphorylation; Potassium; Protein Conformation; Rubidium; Sodium; Sodium-Potassium-Exchanging ATPase; Trypsin | 1982 |
Topological localization of proteolytic sites of sodium and potassium ion stimulated adenosinetriphosphatase.
Topics: Animals; Chemical Phenomena; Chemistry, Physical; Chymotrypsin; Dogs; Erythrocytes; Humans; Kidney; Macromolecular Substances; Ouabain; Rubidium; Sodium-Potassium-Exchanging ATPase; Trypsin | 1983 |
Chymotryptic digestion of the cytoplasmic domain of the beta subunit of Na/K-ATPase alters kinetics of occlusion of Rb+ ions.
Topics: Amino Acid Sequence; Animals; Cell Membrane; Chymotrypsin; Enzyme Inhibitors; Kidney; Kinetics; Membrane Proteins; Molecular Sequence Data; Molecular Weight; Ouabain; Peptide Fragments; Rubidium; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship; Swine | 1996 |
The energy transduction mechanism of Na,K-ATPase studied with iron-catalyzed oxidative cleavage.
Topics: Animals; Catalysis; Chymotrypsin; Iron; Kidney; Microsomes; Ouabain; Phosphates; Phosphorylation; Protein Conformation; Rats; Rubidium; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Vanadates | 1999 |
Entrance port for Na(+) and K(+) ions on Na(+),K(+)-ATPase in the cytoplasmic loop between trans-membrane segments M6 and M7 of the alpha subunit. Proximity Of the cytoplasmic segment of the beta subunit.
Topics: Amino Acid Sequence; Animals; Calcium; Chymotrypsin; Cytoplasm; Dose-Response Relationship, Drug; Enzyme Inhibitors; Isothiuronium; Kidney; Kinetics; Models, Molecular; Molecular Sequence Data; Ouabain; Potassium; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rubidium; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Temperature; Time Factors | 2000 |