The study demonstrates that Ca2+ controls the conformational changes of F-actin induced by myosin subfragment-1 in the presence of 5,5'-dithiobis(2-nitrobenzoic acid) light chains.
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Extends Ca2+ control of F-actin in vitro; leaves open relevance to cardiac muscle regulation in vivo.
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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Borovikov et al. (1982) studied this question.
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