h-89 and methyl-sulfate

h-89 has been researched along with methyl-sulfate* in 1 studies

Other Studies

1 other study(ies) available for h-89 and methyl-sulfate

Article	Year
Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity. Brain research, 1999, May-15, Volume: 828, Issue:1-2 Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of cAMP-dependent protein kinase. Potassium fluoride (KF), 440 mM trimethylamine chloride and exclusion of bovine serum albumin (BSA) decreased the activity of the enzyme, while ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) and the potassium salts of aspartate, gluconate, methylsulfate and monobasic phosphate increased its activity. Addition of KF to the internal solution produced a hyperpolarizing shift in the V1/2 of Ih channel activation, consistent with the KF-induced reduction of protein kinase A activity. Therefore, consideration of the composition of internal solutions is warranted when studying channel physiology by patch-clamp techniques. Topics: Animals; Aspartic Acid; Calcium; Cells, Cultured; Cesium; Chelating Agents; Chlorides; Cyclic AMP-Dependent Protein Kinases; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fluorides; Gluconates; Ion Channels; Isoquinolines; Methylamines; Olfactory Receptor Neurons; Patch-Clamp Techniques; Phosphates; Phosphorylation; Potassium Compounds; Rats; Second Messenger Systems; Serum Albumin, Bovine; Sulfonamides; Sulfuric Acid Esters; Tetraethylammonium	1999

Article

Year

Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity.

Brain research, 1999, May-15, Volume: 828, Issue:1-2

Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of cAMP-dependent protein kinase. Potassium fluoride (KF), 440 mM trimethylamine chloride and exclusion of bovine serum albumin (BSA) decreased the activity of the enzyme, while ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) and the potassium salts of aspartate, gluconate, methylsulfate and monobasic phosphate increased its activity. Addition of KF to the internal solution produced a hyperpolarizing shift in the V1/2 of Ih channel activation, consistent with the KF-induced reduction of protein kinase A activity. Therefore, consideration of the composition of internal solutions is warranted when studying channel physiology by patch-clamp techniques.

Topics: Animals; Aspartic Acid; Calcium; Cells, Cultured; Cesium; Chelating Agents; Chlorides; Cyclic AMP-Dependent Protein Kinases; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fluorides; Gluconates; Ion Channels; Isoquinolines; Methylamines; Olfactory Receptor Neurons; Patch-Clamp Techniques; Phosphates; Phosphorylation; Potassium Compounds; Rats; Second Messenger Systems; Serum Albumin, Bovine; Sulfonamides; Sulfuric Acid Esters; Tetraethylammonium

1999