High affinity binding of the mastoparans by calmodulin

Calmodulin exhibits high affinity, calcium-dependent binding of the mastoparans — a group of cytoactive tetradecapeptides. The dissociation constants for the peptide-calmodulin complexes determined in 0.20 N KCl, 1.0 mM CaCl 2, pH 7.3 are ∼0.3 nM for mastoparan, ∼0.9 nM for mastoparan X, and ∼3.5 nM...

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Veröffentlicht in:Biochemical and biophysical research communications 1983-07, Vol.114 (1), p.50-56
Hauptverfasser: Malencik, Dean A., Anderson, Sonia R.
Format: Artikel
Sprache:eng
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Zusammenfassung:Calmodulin exhibits high affinity, calcium-dependent binding of the mastoparans — a group of cytoactive tetradecapeptides. The dissociation constants for the peptide-calmodulin complexes determined in 0.20 N KCl, 1.0 mM CaCl 2, pH 7.3 are ∼0.3 nM for mastoparan, ∼0.9 nM for mastoparan X, and ∼3.5 nM for Polistes mastoparan. The dissociation constant for the mastoparan-calmodulin complex is the smallest known for any calmodulin binding protein or peptide, suggesting that some type of peptide-calmodulin interaction could be physiologically significant.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(83)91592-9