大鼠睾丸乳酸脱氢酶同工酶－C_4的分离纯化研究

Isolation and Purification of Rat Testicular Lactate Dehydrogenase C_4

采用加热、硫酸铵分段盐析和ＤＥＡＥ－ＳｅｐｈａｄｅｘＡ－５０柱层析，从大鼠睾丸中分离纯化了ＬＤＨ－Ｃ４。比活性提高７８４倍，活性回收率为１２．３％，纯化的ＬＤＨ－Ｃ４经聚丙烯酰胺凝胶电泳（ＰＡＧＥ）鉴定均为一条酶带，位于ＬＤＨ３和ＬＤＨ４之间。

The lactate dehydrogenase isoenzyme C4 of rat testicle was purified with a yield of 12.3%and a raise of specific activity to 784-fold. The purified product was PAGE homogeneous and migrated after LDH3 during electrophoresis.