Purification and partial characterization of a nonprimate growth hormone receptor.

摘要: Pregnant rabbit liver membranes have been shown to possess two types of receptors by displacement analysis, a growth hormone (GH) receptor which binds bovine with an affinity constant (KA) 3 x 10(9) M-1 and ovine prolactin KA 10(8) M-1, (Prl)-specific 5 M-1. The prolactin-specific when solubilized Triton exhibits 4-fold increase in the its while decreases slightly 2 after solubilization. 10-fold difference results has exploited facilitate separation these differential chromatography on human (hGH) gels. is eluted from gel 4 M urea MgCl2 required elute receptor. Conditions optimized, further purification GH preparative isoelectric focusing Sepharose 6B filtration resulted more than 8000-fold This material had Stokes radius 62 A, consistent molecular weight 300,000 gave one main band (75,000 80,000) minor bands sodium dodecyl sulfate (SDS) polyacrylamide gels, could be interpreted as indicating tetrameric was sialoglycoprotein (or closely associated sialoglycoprotein) analytical point 4.6. Specificity studies highly purified confirmed initial hypothesis that this capable binding (bGH) high (oPrl) low affinity, contrast