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Localization and Characterization of a 7.3-kDa Region of Caldesmon Which Reversibly Inhibits Actomyosin ATPase Activity
(East Carolina University, 1992-08-15)
Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and actin and inhibit the binding of myosin subfragments to actin and the subsequent stimulation of ATPase activity. Several ...
Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin.
(East Carolina University, 1999-12)
The purpose of this study was to address the paradox of calponin localization with a-actinin and filamin, two proteins with tandem calponin homology (CH) domains, by determining the effect of these proteins on the binding ...
The Interaction of Caldesmon with the COOH Terminus of Actin
(East Carolina University, 1991-10-25)
Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation experiments that modification of the penultimate cysteine residue of actin significantly weakens its binding to caldesmon ...