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. 1990 Jun 1;268(2):443–448. doi: 10.1042/bj2680443

Hydrodynamic properties of the angiotensin II receptor from bovine adrenal zona glomerulosa.

J J Rondeau 1, N McNicoll 1, E Escher 1, S Meloche 1, H Ong 1, A De Léan 1
PMCID: PMC1131452  PMID: 2363683

Abstract

The bovine adrenal angiotensin II receptor was solubilized with the non-ionic detergent octyl beta-D-glucoside following its binding with the high-affinity antagonist 125I-labelled [Sar1,Ile8]angiotensin II. The complex was sufficiently stable to allow the determination of its hydrodynamic properties. The solubilized receptor migrated on a Superose 6 column as a single peak with a Stokes radius of 5.29 nm. Comparison of sedimentation behaviour through a sucrose density gradient in H2O and 2H2O lead to a partial specific volume of 0.751 ml/g and a sedimentation coefficient (S20,w) of 5.17 S. Combination of gel filtration and sedimentation data indicated that the labelled protein-detergent complex has an Mr of 124,000 and a frictional ratio of 1.42. The Mr of the angiotensin II receptor was estimated as 104,000 kDa after correction for the bound detergent. Photoaffinity cross-linking of 125I-[Sar1, (4-N3)Phe8]angiotension II with bovine adrenal membrane receptor followed by SDS/PAGE under reducing and non-reducing conditions yielded a broad band of Mr 54,000. This suggests that the angiotensin II receptor is a non-covalent dimer in which the two subunits have a similar Mr.

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Selected References

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