Determining the affinity of hormone-receptor interaction.
Characterization of the binding of a hormone to its cognate receptor is a cornerstone of many studies in molecular and cellular endocrinology since this event represents the beginning of a specific cellular response, generally from a highly regulated extracellular messenger. The premise of hormone-receptor interaction follows from the law of mass action describing a reversible second-order reaction, hormone plus receptor, to give a non-covalently associated hormone-receptor complex. From this basic principle, a host of useful experimental parameters are available to the interested investigator. This chapter is focused on development of the experimental and mathematical underpinning of hormone-receptor interaction, with emphasis on a gonadotropin, chorionic gonadotropin (or luteinizing hormone), binding to the luteinizing hormone receptor, a member of the G protein-coupled receptor family. The general concepts and approaches developed herein are, however, valid to most interacting systems.
Puett
David
D
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.
Angelova
Krassimira
K
D000818:Animals; D002460:Cell Line; D006063:Chorionic Gonadotropin / Q000378:metabolism*; D018076:DNA, Complementary; D006801:Humans; D011485:Protein Binding; D051381:Rats; D011974:Receptors, LH / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics
D006063:Chorionic Gonadotropin; D018076:DNA, Complementary; D011974:Receptors, LH