Structure and purification of growth hormone receptors

Cross-linking has also been used to detect GH receptors/binding sites in other tissues and species. The main receptor component detected in rat liver and the human IM9 cell line (which binds human GH specifically) is rather larger (Mt = 100000) than that seen in rabbit liver [35,37], Multiple cross-linked GH-receptor components have been detected in rat hepatocytes, but these are probably all related to aggregates of glycoprotein subunits of Mr 100000 held together by disulphide bonds and non-covalent interactions [37]. 

Partial purification of membrane-bound GH receptors from rabbit liver has been achieved after solubilization with detergents [36,38]. Affinity chromatography on immobilized GH or lectins proved a particularly powerful way of isolating the receptors. However, antibodies raised against the partially-purified receptors failed to block the growth-promoting actions of the hormone. 

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