Purification and characterization of beta-adrenoreceptor rich heart plasma membrane.
A new procedure utilizing saccharose density gradient centrifugation was developed for the purification of beta-adrenergic receptor rich plasma membrane from rabbit heart ventricle tissue. The separation of the plasma membrane fraction from the sarcoplasmic reticulum and mitochondria was verified by conducting binding studies, measuring the activities of marker enzymes, as well as by electron microscopy. It was found that the binding of [3H]-L-dihydroalprenolol is stereospecific in addition to being inhibited by beta-adrenoreceptor agonists and antagonists. Adenylate cyclase retained its responsiveness to beta-agonists and guanine nucleotides.
D015720:5'-Nucleotidase; D000262:Adenylyl Cyclases / Q000032:analysis; D000526:Alprenolol; D000818:Animals; D002462:Cell Membrane / Q000032:analysis / Q000201:enzymology / Q000378:metabolism*; D004082:Dihydroalprenolol; D066298:In Vitro Techniques; D009124:Muscle Proteins / Q000032:analysis; D009206:Myocardium / Q000201:enzymology*; D009708:Nucleotidases / Q000032:analysis; D011817:Rabbits; D011943:Receptors, Adrenergic, beta / Q000302:isolation & purification*; D012508:Sarcolemma / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis
D009124:Muscle Proteins; D011943:Receptors, Adrenergic, beta; D004082:Dihydroalprenolol; D000526:Alprenolol; D009708:Nucleotidases; D015720:5'-Nucleotidase; D000262:Adenylyl Cyclases; D000254:Sodium-Potassium-Exchanging ATPase