Octopus calmodulin. The trimethyllysyl residue is not required for myosin light chain kinase activation

Octopus calmodulin was purified to homogeneity and shown to contain 0.1 residue each of epsilon-N-monomethyl-lysine, epsilon-N-dimethyllysine, and epsilon-N-trimethyllysine/mol. With the exception of this partial methylation and of a single tyrosyl residue, it shared all the characteristic propertie...

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Veröffentlicht in:	The Journal of biological chemistry 1981-01, Vol.256 (1), p.15-18
Hauptverfasser:	Molla, A, Kilhoffer, M C, Ferraz, C, Audemard, E, Walsh, M P, Demaille, J G
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Amino Acids - analysis Animals Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - pharmacology Calmodulin - isolation & purification Calmodulin - pharmacology Dogs Enzyme Activation Kinetics Lysine - analogs & derivatives Molecular Weight Muscles - enzymology Myosins - metabolism Octopodiformes
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