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- W1981124865 abstract "β-Adrenergic binding sites in catfish liver membranes have been characterized by centrifugal assay, using a β-adrenergic receptor antagonist, (−)-[3H]dihydroalprenolol ([3H]DHA). Binding of the radioligand was saturable and reversible. At 22° equilibrium conditions were established in 15 min and the half-time for dissociation of bound [3H]DHA was approximately 4 min. Analysis of binding data was compatible with the existence of two classes of binding sites: a low-affinity site had a Kd of 62.3 nM and a Bmax of 452.0 fmol/mg protein, while the high-affinity site had a Kd of 2.04 nM and a Bmax of 46.7 fmol/mg protein. The dissociation constant of (−)-alprenolol for the β-adrenergic receptors was about 2 nM as determined independently by direct kinetic studies and by inhibition of isoproterenol-stimulated adenylate cyclase activity. Phenylephrine was as potent as other catecholamines in inhibiting [3H]DHA binding, indicating that fish adrenoceptor subtyping is different from that of mammals." @default.
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- W1981124865 date "1979-08-01" @default.
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- W1981124865 title "Mechanisms involved in effects of catecholamines on liver carbohydrate metabolism" @default.
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- W1981124865 doi "https://doi.org/10.1016/0006-2952(79)90684-1" @default.
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