Horm Metab Res 1983; 15(5): 241-245
DOI: 10.1055/s-2007-1018682
Originals

© Georg Thieme Verlag, Stuttgart · New York

Crosslinking of HCG to its Specific Receptor of Porcine Ovarian Membrances

Th. Bauknecht, U. Müller, J. W. Siebers
  • Universitäts-Frauenklinik and Institut für Humangenetik and Anthropologie der Universität Freiburg, Freiburg, Germany
Further Information

Publication History

1981

1982

Publication Date:
14 March 2008 (online)

Summary

HCG receptors of porcine ovarian plasma membranes were loaded with 125I-hCG and covalently crosslinked with glutaraldehyde. The plasma membranes were labeled with tritium. The hCG receptor complex was solubilized in 1% SDS and subsequently chromatographed on Biogel P 300. 40-50% of 125I-radioactivity eluted near the void volume. 3H radioactivity in these fractions indicated the presence of crosslinked hormone receptor complexes. A second minor peak of 125I-radioactivity appeared at 55000 d. A third peak represented subunits of 125I-hCG. Analysis of the Biogel P 300 purified 125I-hCG receptor complex by polyacrylamid gel electrophoresis in sodium dodecyl sulfate resulted in two radioactivity peaks. The main peak corresponded to 90 000-100 000 d, the second peak was calculated to approximately 140 000 d. As a result the majority of the hormone receptor complex has a molecular weight of 90 000-100 000 d. Existence of subunits is discussed