Darré D L, Wallace W R, Dimopoullos G T
J Bacteriol. 1967 Mar;93(3):806-10. doi: 10.1128/jb.93.3.806-810.1967.
Extracts from preparations of partially purified Anaplasma marginale revealed low levels of lactate dehydrogenase (LDH). Enzyme inhibition by immune sera further indicated that A. marginale possesses a protein moiety the same as that of the normal red blood cell (RBC), although data suggested an alteration of LDH(1) from that observed in normal RBC. Bimodal isozyme distribution was detected after electrophoresis of the extracts. One isozyme approached the cathode and the other the anode, and both appeared to be nicotinamide adenine dinucleotide-dependent. Heterogeneity of parasite and host cell isozymes was established on the basis of zone electrophoresis on cellulose acetate strips.
从部分纯化的边缘无形体制剂中提取的物质显示出低水平的乳酸脱氢酶(LDH)。免疫血清对酶的抑制作用进一步表明,边缘无形体具有与正常红细胞(RBC)相同的蛋白质部分,尽管数据表明LDH(1)与正常RBC中观察到的有所不同。提取物电泳后检测到双峰同工酶分布。一种同工酶向阴极移动,另一种向阳极移动,且两者似乎都依赖烟酰胺腺嘌呤二核苷酸。基于醋酸纤维素条上的区带电泳确定了寄生虫和宿主细胞同工酶的异质性。