title: [Intravital research on hydrophobic interactions in protein fibrils using a fluorescence polarization method].
abstract: Fluorescent probe of acridine orange (AO) is known to be bound exclusively by materials of thick protofibril muscle fibres. The dependence of fluorescence anisotropy of AO in frog muscle fibres on the temperature has been studied. It has been found that the fluorophore orientation decreases with temperature, i.e. here the adsorbent cold denaturation takes place. This phenomenon was demonstrated for living, skinned and glycerinated muscle fibres. It shows that hydrophobic interactions contribute much to stabilization of the myosin structure. After contraction of glycerinated muscle fibres at the action of ATP, the AO fluorescence anisotropy grows independently of the temperature which is indicative of structural rearrangements in materials of thick protofibrils upon contraction.
authors.forename: I A
authors.initials: IA
authors.lastname: Gamaleĭ
authors.forename: A B
authors.initials: AB
authors.lastname: Kaulin
mesh_terms: D000165:Acridine Orange; D000818:Animals; D005454:Fluorescence Polarization / Q000379:methods; D005990:Glycerol / Q000494:pharmacology; D009124:Muscle Proteins / Q000378:metabolism*; D009210:Myofibrils / Q000187:drug effects / Q000378:metabolism*; D011896:Rana temporaria; D013696:Temperature
chemical_list: D009124:Muscle Proteins; D000165:Acridine Orange; D005990:Glycerol
vernacular_title: Prizhiznennoe issledovanie gidrofobnykh vzaimodeĭstviĭ v belkovykh fibrillakh poliarizatsionno-fluorestsentnym metodom.