Differentiation of the drug‐binding sites of calmodulin

Calmodulin contains several binding sites for hydrophobic compounds. The apparent specificity of various ‘calmodulin antagonists’ for these sites was investigated. The Ki values for the inhibition of calmodulin‐activated cyclic‐nucleotide phosphodiesterase and myosin light‐chain kinase was determine...

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Veröffentlicht in:	European journal of biochemistry 1987-04, Vol.164 (2), p.411-420
Hauptverfasser:	ZIMMER, Manfred, HOFMANN, Franz
Format:	Artikel
Sprache:	eng
Schlagworte:	2',3'-Cyclic-Nucleotide Phosphodiesterases - antagonists & inhibitors Animals Applied sciences Bepridil Binding Sites calmodulin Calmodulin - antagonists & inhibitors Calmodulin - metabolism drugs Exact sciences and technology In Vitro Techniques Kinetics Myosin-Light-Chain Kinase - antagonists & inhibitors Nimodipine - metabolism Other techniques and industries Pyrrolidines - metabolism Trifluoperazine - metabolism
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