Review
doi: 10.1139/y94-198.
Is phosphorylation the main physiological action of myosin light chain kinase?
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- PMID: 7767881
- DOI: 10.1139/y94-198
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Review
Is phosphorylation the main physiological action of myosin light chain kinase?
Can J Physiol Pharmacol.
1994 Nov.
Abstract
The 155-kDa component of bovine stomach, which exhibits a strong actomyosin (AM) activating activity and a relatively weak myosin light chain kinase (MLCK) activity, has a strong affinity for the actin filament and the actin-binding site is confined to an 80 amino acid residue on its N-terminal side. This affinity may play a crucial role in AM activation. Some reagents preferentially abolish either the AM-activating effect or MLCK activity. In conclusion, MLCK of the 155-kDa component does not play a fundamental role in activating the AM system as far as the in vitro system is concerned. The possible mechanism of AM activation by the component is discussed.
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