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- W2020211915 abstract "The interactions of actin with myosin subfragment-1 and tropomyosin were explored by comparing the reactivities of lysine residues in F-actin alone with those in F-actin complexed to the other proteins. Limited reductive methylation was carried out on F-actin and the F-actin complexes with [14C]HCHO and [3H]HCHO, respectively. After dissociation from the other components, [3H]actin was combined with [14C]actin and 3H/14C of each lysine residue was measured. Myosin subfragment-1 reduced the reactivities of Lys-335 and Lys-372, while tropomyosin reduced those of Lys-237, -325, 327 and -335. When troponin was present in the absence of Ca2+, the effect of tropomyosin on Lys-335 remained the same, but its reactivity was completely restored upon the addition of Ca2+. Thus, the results suggest that different parts of actin are affected by the interaction with myosin subfragment-1 and tropomyosin, but the region containing Lys-335 is commonly affected by the presence of either of them. The change in reactivity is attributable either to a direct steric effect or to an induced conformational effect." @default.
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- W2020211915 date "1982-12-01" @default.
- W2020211915 modified "2023-09-25" @default.
- W2020211915 title "Changes of lysine reactivities of actin in complex with myosin subfragment-1, tropomyosin and troponin" @default.
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- W2020211915 doi "https://doi.org/10.1016/0167-4838(82)90462-9" @default.
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