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PMID: 6847615 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Ca2+-dependent high-affinity complex formation between calmodulin and melittin.

The Biochemical journal ·Vol. 209 ·No. 1 ·1983-01-01 ·Pages 269-72

Comte M, Maulet Y, Cox JA

Abstract

The amphiphatic polypeptide melittin migrates as an equimolar complex with bovine brain calmodulin when monitored by gel disc electrophoresis or gel filtration in the presence of Ca2+, even in 4M-urea. The complex disassociates in the presence of EDTA and urea. The affinity is of the same order as that of calmodulin for its target enzymes, and more than 1000-fold higher than that of calmodulin for basic peptide hormones or hydrophobic drugs. The activation of brain phosphodiesterase by calmodulin is inhibited by melittin. The kinetics of inhibition suggest competition between the enzyme and melittin for calmodulin. The calmodulin-melittin interaction may constitute a model for that existing between calmodulin and its target enzymes.

MeSH Terms
Animals Bee Venoms/metabolism Calcium/pharmacology Calcium-Binding Proteins/metabolism Calmodulin/metabolism Cattle Chromatography, Gel Electrophoresis, Disc Macromolecular Substances Melitten/metabolism,pharmacology Phosphodiesterase Inhibitors/pharmacology Protein Binding
Chemicals
Bee Venoms Calcium-Binding Proteins Calmodulin Macromolecular Substances Phosphodiesterase Inhibitors Melitten Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Comte M
Maulet Y
Cox J A
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27 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2090269
Published
1983-01-01
Pages
269-72
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1154084
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2090269 PMC Full Text View journal details
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