[Effect of caldesmon on the type of conformation changes in F-actin induced by the binding of myosin 1 subfragment].
The effect of caldesmon on the conformational changes of F-actin caused by myosin subfragment 1 (S-1) binding was studied, using the polarized microfluorimetry method. It was demonstrated that the polarized fluorescence of rhodaminil-phalloin specifically bound to F-actin of pure actin filaments as well as of tropomyosin-containing actin filaments changes as a result of binding to S-1. The nature of these changes depends on the presence of caldesmon in the filaments. Caldesmon was supposed to modify the conformational changes in F-actin induced by S-1.
Borovikov
Iu S
IuS
Galazkiewicz
B
B
Dabrowska
R
R
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D005456:Fluorescent Dyes; D009132:Muscles / Q000378:metabolism*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D002148:Calmodulin-Binding Proteins; D005456:Fluorescent Dyes; D015879:Myosin Subfragments; D010446:Peptide Fragments; D009218:Myosins
Vliianie kal'desmona na kharakter konformatsionnykh izmeneniĭ F-aktina, indutsirovannykh sviazyvaniem subfragmenta 1 miozina.