[Resistance to heating and trypsin of glutamate dehydrogenase from liver mitochondria of frogs differing in thermotaxis].
The resistances to heat and trypsin hydrolysis served as indirect indices of conformational flexibility of glutamate dehydrogenase molecules. No difference in heat resistance was found between crystalline eletrophoretically homogeneous preparations of glutamate dehydrogenase from liver mitochondria of two species of frogs, the more southern Rana ridibunda and the more northern R. temporaria. However, glutamate dehydrogenase from R. ridibunda is digested by trypsin at a lower rate than that from R. temporaria, which may be explained by its lower conformational flexibility. Therefore positive correlation between conformational flexibility of glutamate dehydrogenase and mean ambient temperature of the species studied is revealed only with respect to resistance to proteolysis.
D000818:Animals; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006358:Hot Temperature; D008930:Mitochondria, Liver / Q000201:enzymology*; D011896:Rana temporaria / Q000378:metabolism; D011898:Ranidae; D013045:Species Specificity; D014357:Trypsin / Q000378:metabolism
D005969:Glutamate Dehydrogenase; D014357:Trypsin
Ustoĭchivost' k nagrevu i tripsinu glutamatdegidrogenazy mitokhondriĭ pecheni liagushek, otlichaiushchikhsia po teploliubivosti