[Nature of the changes in the activity of water-soluble enzymes in exposure of muscles to harmful agents. IV. The study of hexokinase extractability from intact and altered muscles].
A possibility of hexokinase binding with actomyosin in skeletal muscles of Rana temporaria L., and the effect of thermal alteration (15 min at 36, 37, 38, 40 and 42 degrees C) on the binding were studied. Solutions of KCl (0.075 M and 0.15 M) extract more hexokinase from intact and altered muscles than does an non-electrolyte medium. Hexokinase freely dissolved in hyaloplasm is extracted in non-electrolyte medium. Hexokinase bound with structural components of the muscle cell is extracted upon the increase in ionic force of the extractant. The solubilizing effect of electrolytes on hexokinase is higher in alterated muscles than in the intact muscles indicating the increase in hexokinase binding under thermal alteration. Actomysin isolated from muscles reveals hexokinase activity. In reprecipitated actomyosin, the larger part of its hexokinase remains in actomyosin gel, the level of hexokinase activity not depending on the number of reprecipitation procedures or on the volume of washing solution. Hexokinase in actomyosin gel is less stable to the thermal action than in water supernatant of muscle extract. This may be due to the increase in hexokinase binding with actomiosin whose sorption activity increases under the thermal denaturation.
D000205:Actomyosin / Q000378:metabolism; D000818:Animals; D005782:Gels; D006593:Hexokinase / Q000378:metabolism*; D006358:Hot Temperature; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D011485:Protein Binding / Q000187:drug effects; D011896:Rana temporaria; D012995:Solubility; D013696:Temperature; D014508:Urea / Q000494:pharmacology
D005782:Gels; D014508:Urea; D000205:Actomyosin; D006593:Hexokinase
K voprosu o prirode izmeneniĭ aktivnosti vodorastvorimykh fermentov pri deĭstvii na myshtsy povrezhdaiushchikh agentov. IV. Izuchenie izvlekaemosti geksokinazy iz intaktnykh i al'terirovannykh myshts.