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- W1788082166 abstract "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 both in the presence and absence of tropomyosin. Furthermore, as revealed by fluorescence measurements, caldesmon increases the exposure of the COOH-terminal region of actin to the solvent. This effect of caldesmon, like its inhibitory effect on actomyosin ATPase activity, is enhanced in the presence of tropomyosin. Proteolytic removal of the last three COOH-terminal residues of actin, containing the modified cysteine residue, restores the normal binding between caldesmon and actin. These results establish a correlation between the binding of caldesmon to actin and the conformation of the COOH-terminal region of actin and suggest an indirect rather than direct interaction between caldesmon and this part of actin." @default.
- W1788082166 created "2016-06-24" @default.
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- W1788082166 date "1991-10-01" @default.
- W1788082166 modified "2023-09-28" @default.
- W1788082166 title "The interaction of caldesmon with the COOH terminus of actin." @default.
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- W1788082166 doi "https://doi.org/10.1016/s0021-9258(18)54883-3" @default.
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