[2] Wheat Germ Lectin-Sepharose Affinity Adsorption Assay for the Soluble Glucagon Receptor

Ravi Iyengar, John T. Herberg

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

This chapter explains that the hepatic glucagon-sensitive adenylyl cyclase has been widely used as a model system to study the signal transduction process in adenylyl cyclase systems. However, purification of the receptor has not been possible up to now. This is due to lack of availability of a reliable assay for the solubilized receptor. The chapter also explains that the methods commonly used for other soluble receptors, such as gel filtration and polyethylene glycol precipitation, have not proven useful for assaying the glucagon receptor due to unacceptably high backgrounds. The chapter attempts to develop a simple assay that would be based on a unique property of the receptor and explains that in the past few years, it has been found that many hormone receptors are glycoproteins and the hormone–receptor complex could be specifically adsorbed onto the lectin-Sepharose, while the free hormone would remain in solution. The solid phase containing the hormone–receptor complex could be separated from the free hormone by low-speed centrifugation and removal of the supernatant. The hormone–receptor complex formed could then be estimated by counting the lectin-Sepharose in a gamma counter.

Original languageEnglish
Pages (from-to)13-20
Number of pages8
JournalMethods in Enzymology
Volume109
Issue numberC
DOIs
StatePublished - 1 Jan 1985

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