[Structural changes in the contractile proteins of muscle fiber studied by polarization ultraviolet fluorescence microscopy. IX. The effect of the pH and ionic strength of the solution on the conformational restructurings of F-actin induced by the binding of heavy meromyosin].
The dependence of F-actin conformational changes induced by the F-actin-HMM complex on pH and ionic strength was found by polarized ultraviolet fluorescence microscopy. It is discovered that pH affects sufficiently the cooperativity of F-actin structural changes, while the ionic strength affects their depth. The actomyosin complex was supposed to be at least in two structural states, differing in their orientation as well as in flexibility of F-actin monomers.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D008856:Microscopy, Fluorescence; D008859:Microscopy, Polarization; D008860:Microscopy, Ultraviolet; D009124:Muscle Proteins / Q000378:metabolism*; D015879:Myosin Subfragments / Q000378:metabolism*; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D009124:Muscle Proteins; D015879:Myosin Subfragments
Izuchenie strukturnykh izmeneniĭ sokratitel'nykh belkov myshechnogo volokna s pomoshch'iu poliarizatsionnoĭ ul'trafioletovoĭ fluorestsentnoĭ mikroskopii. IX. Vliianie pH i ionnoĭ sily rastvora na konformatsionnye perestroĭki F-aktina, indutsirovannye sviazyvaniem tiazhelogo meromiozina.