[The nature of the changes in the activity of water-soluble enzymes in action on the muscles of damaging agents. VI. Glyceraldehyde-3-phosphate dehydrogenase binding and enzyme adsorption by F-actin in ghost muscle fiber].
A possibility of binding glyceraldehyde-3-phosphate dehydrogenase (GAPhDG) in frog (Rana temporaria L.) skeletal muscles was studied by measuring its solubilization in 0.15 M KCl and by its presence in isolated actomyosin. Using a 0.15 M KCl solution, more GAPhDG was extracted from intact muscles and muscles treated with heat at 38, 42 and 46 degrees C for 15 min than in a non-electrolyte medium. Actomyosin isolated from muscles reveals GAPhDG activity which cannot be removed by actomyosin reprecipitation. In myosin-, troponin- and tropomyosin-free single glycerinated muscle fibres (ghost fibres) GAPhDG absorption to F-actin was shown. It is suggested that under thermal injure of muscle cells, the increase in GAPhDG binding with thermolabile proteins of actomyosin complex may occur.
Stabrovskaia
V I
VI
D000199:Actins / Q000378:metabolism*; D000205:Actomyosin / Q000302:isolation & purification / Q000378:metabolism; D000327:Adsorption; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D006358:Hot Temperature; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011896:Rana temporaria; D012995:Solubility
D000199:Actins; D000205:Actomyosin; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
K voprosu o prirode izmeneniĭ aktivnosti vodorastvorimykh fermentov pri deĭstvii na myshtsy povrezhdaiushchikh agentov. VI. Sviazyvanie glitseral'degid-3-fosfatdegidrogenazy v myshtse i adsorbtsiia fermenta F-aktinom tenevogo myshechnogo volokna.