Haque M, Siddiqi A H, Siddiqui J
Department of Zoology, Aligarh Muslim University, India.
Int J Parasitol. 1990 Dec;20(8):1113-5. doi: 10.1016/0020-7519(90)90060-z.
Polyacrylamide gel electrophoresis of the two digenetic trematodes, Gigantocotyle explanatum from the liver and Gastrothylax crumenifer from the rumen of the water buffalo, Bubalus bubalis revealed the presence of at least six and seven isoenzymes of lactate dehydrogenase (LDH), respectively in a partially purified enzyme preparation. The respective host tissues showed five isoenzymes of LDH, which are characteristic to the vertebrates. Both parachloromercuribenzoate and iodoacetate affected the LDH activity of the parasites and host tissues differently. Spectrophotometric analysis also showed different specific activity and susceptibility to the action of thiol inhibitors. The host LDH was quite stable at 57 degrees C for 30 min, but that of the parasites was less stable.
对来自水牛（Bubalus bubalis）肝脏的巨大阔盘吸虫（Gigantocotyle explanatum）和来自瘤胃的瘤胃腹袋吸虫（Gastrothylax crumenifer）这两种复殖吸虫进行聚丙烯酰胺凝胶电泳分析，结果显示在部分纯化的酶制剂中，分别至少存在六种和七种乳酸脱氢酶（LDH）同工酶。各自的宿主组织显示出五种LDH同工酶，这是脊椎动物所特有的。对氯汞苯甲酸和碘乙酸对寄生虫和宿主组织的LDH活性有不同影响。分光光度分析还显示出不同的比活性以及对硫醇抑制剂作用的敏感性。宿主的LDH在57摄氏度下30分钟相当稳定，但寄生虫的LDH稳定性较差。
