American Cyanamid Company

University of Virginia Patent Foundation

John R Zysk

Michael Oliver Thorner

Bruce D Gaylinn

Kevin R Lynch

Jeffrey K Harrison

Cecil Mark Eppler

Hong-Ming Shieh

Martin John Corbett

William R Baumbach

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromotography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor.

Isolation and characterization of the growth hormone releasing hormone

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromatography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line.

Cloning of a gene encoding for the growth hormone releasing hormone

Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromotography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line.

Nucleic acid encoding the growth hormone releasing hormone receptor

Nucleic acid molecule encoding the porcine growth hormone receptor

The invention relates to a purified somatostatin receptor which is purified at least about 30,000-fold over the receptor which is membrane-bound. The invention also provides pharmaceutical compositions containing the receptor and antibodies to the receptor.

Purified active somatostatin receptor

The receptor:ligand complex is applied to a solid phase substrate which binds the complex by specifically binding the ligand. The receptor is dissociated from the substrate bound receptor:ligand complex with an eluant capable of releasing the receptor from the ligand and leaving the ligand bound to the solid phase substrate. GTP containing eluants are effective. The receptor is recovered from the eluate and optionally subjected to further purification.

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Frenchtown, NJ, United States of America

John R Zysk