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PMID: 3159185 Published · ppublish English Journal Article

High-affinity binding of forskolin to rat brain membranes.

Advances in cyclic nucleotide and protein phosphorylation research ·Vol. 19 ·1985-00-00 ·Pages 125-35

Seamon KB, Daly JW

Abstract

High-affinity forskolin binding sites in brain membranes have been identified that have structure-activity characteristics compatible with forskolin's site of action at the adenylate cyclase enzyme. It is proposed that these high-affinity binding sites are associated with an activated complex of the catalytic protein and the alpha s subunit. Quantitation of high-affinity forskolin binding sites may provide a direct measure of the amount of adenylate cyclase that has the potential to be regulated by stimulatory hormones and the Ns subunit.

MeSH Terms
Adenylyl Cyclases/metabolism Animals Brain/metabolism Cations, Divalent/pharmacology Colforsin Diterpenes/metabolism Edetic Acid/pharmacology Enzyme Activation Fluorides/pharmacology GTP-Binding Proteins/metabolism Guanylyl Imidodiphosphate/pharmacology Kinetics Protein Binding/drug effects Rats Structure-Activity Relationship Synaptosomes/metabolism Temperature
Chemicals
Cations, Divalent Diterpenes Colforsin Guanylyl Imidodiphosphate Edetic Acid GTP-Binding Proteins Adenylyl Cyclases Fluorides
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Seamon K B
Daly J W
Article Info
Journal
Advances in cyclic nucleotide and protein phosphorylation research
Abbr.
Adv Cyclic Nucleotide Protein Phosphorylation Res
ISSN
0747-7767
Published
1985-00-00
Pages
125-35
Language
English
Region
United States
NLM ID
8404639
Subset
IM
External Links
PubMed source
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