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A homologous population of specific angiotensin II receptors is present on the cell surface of isolated rabbit hepatocytes. The binding characteristics of [³H]angiotensin II to the cells were: association rate constant (K₊₁) 0·08 l/nmol per min and dissociation rate constant (K_–1) 1·9/min, yielding a dissociation constant (K_d) of 24 nmol/l. A very similar K_d (32 nmol/l) has been derived from saturation binding data which indicate a maximal binding capacity of about 200 000 sites/cell.

Analysis of the association binding data to purified liver plasma membranes indicated a K_d of 6 nmol/l in the absence and 30 nmol/l in the presence of GTP. Dissociation was clearly dependent upon the presence of the nucleotide, which shifted the K_–1 from 0·12/min to 0·42/min.

The studied binding sites are very likely to be involved in the glycogenolytic action of angiotensin II, since a highly significant correlation was established between the biological activity (activation of glycogen phosphorylase) and the binding affinity of a series of agonistic analogues.

The reported characteristics of the rabbit hepatic angiotensin II receptors show much similarity with those of rat liver.

Journal of Endocrinology (1989) 123, 131–136

This article has been cited by other articles:

				T. L. Goodfriend, M. E. Elliott, and K. J. Catt Angiotensin Receptors and Their Antagonists N. Engl. J. Med., June 20, 1996; 334(25): 1649 - 1655. [Full Text] [PDF]