Both α and β Subunits of Human Choriogonadotropin Photoaffinity Label the Hormone Receptor

Details Both α and β Subunits of Human Choriogonadotropin Photoaffinity Label the Hormone Receptor Both α and β Subunits of Human Choriogonadotropin Photoaffinity Label the Hormone Receptor

Sep 1981

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1981pnas...78.5465j&link_type=abstract

Proceedings of the National Academy of Sciences of the United States of America, Volume 78, Issue 9, pp. 5465-5469

Computer Science

1

Scientific paper

It has been shown that a photoactivable derivative of human choriogonadotropin (hCG) labels the lutropin receptor on porcine granulosa cells [Ji, I. & Ji, T. H. (1980) Proc. Natl. Acad. Sci. USA 77, 7167--7170]. In an attempt to identify which of the hCG subunits labeled the receptor, three sets of different hCG derivatives were prepared. In the first set, hCG was coupled to the N-hydroxysuccinimide ester of 4-azidobenzoylglycine and radioiodinated. In the second set, only one of the subunits was radioiodinated, but both subunits were allowed to react with the reagent. In the third set, both the reagent and [125I]iodine were coupled to only one of the subunits. The binding activity of each hormone derivative was comparable to that of 125I-labeled hCG. After binding of these hormone derivatives to the granulosa cell surface, they were photolyzed. After solubilization, autoradiographs of sodium dodecyl sulfate/polyacrylamide gels of each sample revealed a number of labeled bands; the hCG derivatives containing 125I-labeled α subunit produced four bands (molecular weights 120,000± 6,000, 96,000± 5,000, 76,000± 4,000, and 73,000± 4,000) and those containing 125I-labeled β subunit produced three bands (molecular weights 106,000± 6,000, 88,000± 5,000, and 83,000± 4,000). Results were the same when the hormone--receptor complexes were solubilized in 0.5% Triton X-100 and then photolyzed or when the hormone was derivatized with a family of reagents having arms of various lengths. We conclude that both the α subunit and the β subunit of hCG photoaffinity labeled certain membrane polypeptides and that these polypeptides are related to the hormone receptor.

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