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Radiation Inactivation (Target Size Analysis) of the Gonadotropin-Releasing Hormone Receptor: Evidence for a High Molecular Weight Complex^*

P. MICHAEL CONN and J. CRAIG VENTER

Department of Pharmacology, Duke University Medical Center Department of Pharmacology, University of Iowa College of Medicine Durham, North Carolina 27710; Iowa City, Iowa 52242;
Department of Molecular Immunology, Roswell Park Memorial Institute Buffalo, New York 14263

Address all correspondence and requests for reprints to: P. Michael Conn, Department of Pharmacology, University of Iowa College Medicine, Iowa City, Iowa 52242.

Abstract

In the present study we used radiation inactivation (target size analysis) to measure the functional mol wt of the GnRH receptor while it is still a component of the plasma membrane. This technique is based on the observation that an inverse relationship exists between the dose-dependent inactivation of a macromolecule by ionizing radiation and the size of that macromolecule. This method demonstrates a mol wt of 136,346 ± 8,120 for the GnRH receptor. This estimate is approximately twice that obtained (60,000) by photoaffinity labeling with a radioactive GnRH analog followed by electrophoresis under denaturing conditions and, accordingly, presents the possibility that the functional receptor consists of a high mol wt complex in its native state. The present studies indicate that the GnRH receptor is either a single weight class of protein or several closely related weight classes, such as might occur due to protein glycosylation. (Endocrinology 116: 1324-1326, 1985)

Footnotes

^* This work was supported by Grants HD-19899 (to P.M.C.) and HL-31178 and AI-19346 (to J.C.V.).

Present address: Section on Receptor Biochemistry, Laboratory of Neurophysiology, NINCDS, NIH, Bethesda, MD 20205.

Received September 25, 1984.

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