Specific binding of 125I-labelled human somatotropin was demonstrated in microsomal membranes (microsomes) from rat and rabbit kidneys. Female rabbit kidney microsomes showed the highest binding activity and were used for further study. The association of 125I-labelled human somatotropin was time- and temperature-dependent and the binding reaction was reversible. Scatchard analysis of saturation data indicated a dissociation equilibrium constant, KD, of 56 pM and a binding capacity of 37 fmol per mg of protein. Similar results were obtained from competition experiments. Binding of 125I-labelled human somatotropin to the microsomes was specifically inhibited by hormones with lactogenic activity. The binding sites, as well as 125I-labelled human somatotropin, were not inactivated on incubation. Treatment of the microsomes with trypsin and chymotrypsin decreased the specific binding by over 90%. Preheating of the microsomes at 55 degrees C for 15 min abolished 50% of the specific binding activity.
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Research Article| November 15 1981
Human somatotropin binding to rabbit kidney microsomal fraction
J S Bonifacino ;
Biochem J (1981) 200 (2): 257–264.
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L P Roguin, S H Sánchez, J S Bonifacino, A C Paladini; Human somatotropin binding to rabbit kidney microsomal fraction. Biochem J 15 November 1981; 200 (2): 257–264. doi: https://doi.org/10.1042/bj2000257
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