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Solubilization and affinity labeling of a dihydropyridine binding site from skeletal muscle: effects of temperature and diltiazem on [3H]dihydropyridine binding to transverse tubules |
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| Authors: | T L Kirley A Schwartz |
| Institution: | Department of Pharmacology and Cell Biophysics University of Cincinnati College of Medicine Cincinnati, Ohio 45267-0575 USA |
| Abstract: | Effects of temperature and d-cis-diltiazem (DTZ) on 3H]nitrendipine (NTD) and 3H]nimodipine (NIM) binding to skeletal muscle t-tubular membranes were studied. A decrease in temperature from 37 degrees C to 10 degrees C decreased KD and increased Bmax slightly. DTZ increased binding by increasing Bmax under all conditions and also decreased KD for NTD at 37 degrees C. The binding protein labeled with 3H]isothiocyanate dihydropyridine revealed a molecular weight of 36,000. The binding site for NTD was solubilized by deoxycholate and dihydropyridine binding was still stimulated by DTZ in the solubilized form. |
| Keywords: | t-tubule(s) transverse tubule(s) NTD nitrendipine NIM nimodipine DTZ d-cis-diltiazem dissociation constant maximal number of binding sites DHP dihydropyridine DHPNCS isothiocyanate labeled dihydropyridine PEG polyethelene glycol (Na) DOC (sodium) deoxycholate SR sarcoplasmic reticulum ATPase adenosine triphosphatase SDS-PAGE sodium dodecyl sulfate polyacrylamide gel electrophoresis SM surface membranes EGTA ethylene glycol-bis-(β-aminoethylether) N N′-Tetraacetic acid |
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