title: Significance of the variation in isozymes of liver lactate dehydrogenase with thermal acclimation in goldfish--I. Thermostability and temperature dependency.
abstract: 1. Total and isozyme properties as well as isozyme pattern were examined in liver lactate dehydrogenase (LDH) from goldfish acclimated to different temperatures. 2. LDH of warm-acclimated fish were thermostable and exhibited higher Q10 in low temperature range as compared with that of co ld-acclimated fish. 3. The relative activities of LDH-1, LDH-2 and LDH-3, which were more thermostable, increased and LDH-4 and LDH-5, which were more heat sensitive, decreased during warm acclimation. Q10 in the low temperature range for LDH-5 was lower than that for LDH-1.
mesh_terms: D000064:Acclimatization; D000818:Animals; D003530:Cyprinidae / Q000378:metabolism*; D004588:Electrophoresis, Cellulose Acetate; D004795:Enzyme Stability; D006054:Goldfish / Q000378:metabolism*; D006706:Homeostasis; D006358:Hot Temperature; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000032:analysis* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase