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  • Title: Effect of Ca2+ binding to 5,5'-dithiobis(2-nitrobenzoic acid) light chains on conformational changes of F-actin caused by myosin subfragment-1.
    Author: Borovikov YS, Levitskii DI, Kirillina VP, Poglazov BF.
    Journal: Eur J Biochem; 1982 Jul; 125(2):343-7. PubMed ID: 7117236.
    Abstract:
    The fluorescent ADP analogue, 1:N6-ethenoadenosine 5'-diphosphate, was incorporated into F-actin in a myosin-free ghost single fibre. Polarized fluorescence measurements of tryptophan residues and 1:N6-ethenoadenosine 5'-diphosphate were performed under a microspectrophotometer to investigate the conformation of F-actin and the changes induced in it by myosin subfragment-1 with 5,5'-dithiobis(2-nitrobenzoic acid) light chains and without them. A relation was found between the conformational state of F-actin and the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains. The conformational changes were shown to be controlled by Ca2+ in the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains.
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