Photoaffinity labeling of human chorionic gonadotropin-binding sites in rat ovarian plasma membranes.

This publication has 12 references indexed in Scilit:

• Isolation of the luteinizing hormone-chorionic gonadotropin receptor in high yield from bovine corpora lutea. Molecular assembly and oligomeric nature.
  Journal of Biological Chemistry, 1983
• Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase. Structural alterations in the beta-adrenergic receptor revealed by photoaffinity labeling.
  Journal of Biological Chemistry, 1982
• Covalent crosslinking of human chorionic gonadotropin to its receptor in rat testes.
  Proceedings of the National Academy of Sciences, 1981
• Macromolecular photoaffinity labeling of the lutropin receptor on granulosa cells.
  Proceedings of the National Academy of Sciences, 1980
• Purification of luteinizing hormone receptor and its subunit structure
  Biochemical and Biophysical Research Communications, 1980
• Studies on the Receptor for Luteinizing Hormone in a Purified Plasma Membrane Preparation from Rat Ovary*
  Endocrinology, 1980
• Properties of LH-sensitive adenylate cyclase in purified plasma membranes from rat ovary
  Molecular and Cellular Endocrinology, 1978
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
  Annals of the New York Academy of Sciences, 1949