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 |
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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
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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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(83)91592-9 |