中国大鲵乳酸脱氢酶同工酶研究──Ⅱ动力学性质

STUDIES ON LACTATE DEHYDROGENASE ISOZYMES OF MEGALOBATRACHUS DAVIDIANUS (BLANCHARD)Ⅱ. KINETICS

Department of Biology, Huaibei Teachers College, Huaibei, 235000;
2. Department of Biology, Shanxi University, Xian, 710062

摘要: 利用垂直板聚丙烯酰胺凝胶电泳法分离大鲵[Megalobatrachus davidianus(Blanchard)]乳酸脱氢酶同工酶。研究了各同工酶的最适pH、最适温度、热稳定性、米氏常数、底物抑制等动力学性质。
- LDH同工酶 /
- 动力学性质 /
- 大鲵
Abstract: The optimum pH of LDH1 isozyme of M. davidianus was 7.2 (pyruvate as substrate) and 9.6 (L-lactate as substrate) and LDH5 6.4 (pyruvate as substrate) and 10.0 (L-lactate as substrate). The optimtun temperature of LDH1 was above 37℃ and LDH5 37℃. The thermal stability of LDH1 is higher than that of LDH5. The Km of LDH1 was 2×10-4mol/L (pyruvate as substrate) and 8.5×10-3mol/L (L-lactate as substrate) and LDH5 3×10-4 mol/L (pyruvate as substrate) and 31.2×10-3mol/L (L-lactate as substrate). The LDH1 reached maximum activity at approximately 0.5 mmol/L pyruvate or 50 mmol/L L-ractate, whereas the LDH5 reaches makimum activity at approximately 1.0 mmol/L pyruvate or 300 mmol/L L-lactate.
- LDH isozyme /
- Kinetics /
- Megalobatrachus davidianus