Analysis of growth hormone and lactogenic binding sites cross-linked to iodinated human growth hormone.
作者： J. P. HUGHES , J. S. A. SIMPSON , H. G. FRIESEN
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摘要: GH (GHR) and lactogenic receptors were analyzed after use of the cross-linking reagent ethylene glycol bis- (succinimidyl succinate) to attach covalently iodinated human (hGH) binding proteins 1) on intact IM-9 lymphocytes, 2) in a partially purified GHR preparation from rabbit liver, 3) crude microsomal fractions mammary gland, rat liver. The latter two preparations contain primarily receptors, whereas lymphocytes liver preparations, predominate. Cross-linked [125I]hGH-receptor complexes solubilized, reduced, separated sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Analysis cross-linked [125I]hGH fraction showed specifically labeled complex with an estimated molecular weight (mol wt) 75K. A slightly lower mol wt (71K) was determined for preparation. In contrast relatively low comple...
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