Predicted beta-turns in peptide and glycopeptide anti-freezes |
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Authors: | M H Loucheux-Lefebvre |
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Institution: | 1. Nencki Institute of Experimental Biology, Department of Biochemistry of Nervous System and Muscle, 3, Pasteur Street, 02-093, Warsaw, Poland;2. Muscle Biology Group, 309 Agricultural Sciences Building, The University of Arizona, Tucson, Arizona, 85721 USA |
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Abstract: | A myosin light chain kinase has been obtained in a partially purified form from human blood platelets and bovine brain. The kinase from both sources required Ca2+ and the modulator protein for its activity. The subunit molecular weight is approximately 105,000 daltons. These kinases are therefore similar to the smooth muscle kinase (Dabrowska, R., Aromatorio, D., Sherry, J. M. F., and Hartshorne, D. J. (1977) Biochem. Biophys. Res. Commun. 78, 1263–1272). It is suggested that the role of the myosin light chain kinase is similar in both muscle and non-muscle cells and serves to activate the contractile apparatus, via the phosphorylation of myosin, in response to an increase in the intracellular free Ca2+ concentration. |
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Keywords: | Requests for reprints to be addressed to D J Hartshorne |
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