Effect of Ca2+ Binding to 5,5'-Dithiobis(2-nitrobenzoic aoid) Light Chains on Conformational Changes of F-Actin Caused by Myosin Subfragment-1
Open Access
- 1 July 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 125 (2), 343-347
- https://doi.org/10.1111/j.1432-1033.1982.tb06689.x
Abstract
The fluorescent ADP analog 1:N6-ethenoadenosine 5''-diphosphate was incorporated into F-actin in a myosin-free ghost single [rabbit] fiber. 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) L 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) L chains. The conformational changes were controlled by Ca2+ in the presence of 5,5''-dithiobis(2-nitrobenzoic acid) L chains.This publication has 36 references indexed in Scilit:
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