Effect of Ca2+ on conformation of actin in the F-actin--heavy meromyosin complex.
The polarized fluorescence of intrinsic tryptophan residues and the birefringence of ghost muscle fibres of rabbit were measured during thin filaments binding to heavy meromyosin containing 5,5'-dithiobis [2-nitrobenzoic acid] light chains and to those devoid of them with a view of investigating conformational changes in F-actin. Ca2+ binding to heavy meromyosin containing 5,5'-dithiobis [2-nitrobenzoic acid] light chains was shown to affect the character of these changes during the formation of the F-actin - heavy meromyosin complex.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001718:Birefringence; D002118:Calcium / Q000494:pharmacology*; D003599:Cytoskeleton / Q000378:metabolism; D046911:Macromolecular Substances; D009132:Muscles / Q000378:metabolism; D015879:Myosin Subfragments / Q000378:metabolism*; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D014364:Tryptophan; D002118:Calcium