[Isolation and characteristics of dihydropyridine calcium antagonist receptor from rabbit skeletal muscles].
Up to 80% of the dihydropyridine receptor is solubilized from transverse tubules of rabbit skeletal muscle by 3-[(3-cholamidopropyl)-dimethylammonium]-2-oxy-1-propane sulfonate (CHAPSO). The DHP receptor is an oligomeric complex made up of two subunits with molecular masses of 160 and 53 kD as shown by DHP-Sepharose affinity chromatography and SDS gel electrophoresis of specifically eluted proteins. The reduction of disulfide bridges of the 160 kD subunit is accompanied by a decrease in its apparent molecular mass up to 125 kD. A method is proposed for preparative isolation of the DHP receptor which is based on ion-exchange chromatography and WGA-Sepharose chromatography. Individual subunits of DHP receptor were isolated by Sepharose 4B gel filtration in SDS; their amino acid composition was determined. Both the 160 and 53 kD subunits are N-glycosylated, and the oligosaccharide portions make up to 7.5% and 6.6%, respectively.
Soldatov
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D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002121:Calcium Channel Blockers / Q000378:metabolism*; D015220:Calcium Channels; D002846:Chromatography, Affinity; D004095:Dihydropyridines / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D009132:Muscles / Q000032:analysis*; D011817:Rabbits; D011978:Receptors, Nicotinic / Q000302:isolation & purification* / Q000378:metabolism; D012995:Solubility
D000596:Amino Acids; D002121:Calcium Channel Blockers; D015220:Calcium Channels; D004095:Dihydropyridines; D011978:Receptors, Nicotinic
Vydelenie i kharakteristika retseptora digidropiridinovykh kal'tsievykh antagonistov iz skeletnoĭ myshtsy krolika.