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. 1983 Jan 1;209(1):269–272. doi: 10.1042/bj2090269

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

M Comte, Y Maulet, J A Cox
PMCID: PMC1154084  PMID: 6847615

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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