[The nature of changes in the activity of water-soluble enzymes during the action of injurious agents on the muscles. V. A study of the extractability of lactate dehydrogenase from intact and altered muscles].
A study was made of lactate dehydrogenase (LDH) extractability from intact and thermally injured muscles of Rana temporaria L. in the 0.15 M KCl solution and in the non-electrolyte medium. A 15 minute incubation of intact muscles and those treated with heat at 38, 42, 44 and 46 degrees C in the 0.15 M KCl solution led to a much higher extraction of LDH than in the non-electrolyte medium. Following heating at 38 degrees C, causing irreversible injury of muscles, the LDH extractability in the non-electrolyte medium is seen to fall, whereas in the 0.15 M KCl solution it remained at the same level as after LDH extraction from intact muscles. The decrease in LDH extractability in non-electrolyte medium from thermally injured muscles may be due to the increase in LDH binding with thermolabile structural components of muscle. One of the components of muscle cell, known to bind LDH, is actomyosin, since it is isolated from muscles together with LDH, which cannot be removed by actomyosin reprecipitation or by increasing the volume of washing solution.
Stabrovskaia
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D000205:Actomyosin / Q000378:metabolism; D000327:Adsorption; D000818:Animals; D004795:Enzyme Stability; D006358:Hot Temperature; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D011896:Rana temporaria; D012995:Solubility; D013696:Temperature
D000205:Actomyosin; D007770:L-Lactate Dehydrogenase
K voprosu o prirode izmeneniĭ aktivnosti vodorastvorimykh fermentov pri deĭstvii na myshtsy povrezhdaiushchikh agentov. V. Izuchenie izvlekaemosti laktatdegidrogenazy iz intaktnykh i al'terirovannykh myshts.