恶性疟原虫乳酸脱氢酶(LDH—p)得以与人红细胞LDH(LDH—r)分开并纯化,并对他们的特性进行了比较。结果表明,LDH—p和LDH—r均可利用烟酰胺腺嘌呤二核苷酸(nicotinamide adenine dinucleotide,NAD),促进乳酸盐与丙酮酸盐的相互转化;而只有LDH—p可更快速地利用NAD类似物—乙酰吡啶腺嘌呤二核苷酸(acetyl pyridine adenine dinucteotide,APAD)完成同一反应,LDH—r不能利用APAD。在PAGE电泳中,NAD使LDH—p和LDH—r均被染色,前者为一条带,后者为三条不同的带;当以APAD染色时,只有LDH—p被更深地染色,LDH—r带均未显色。以上表明,两种LDH具有明显不同的生化、物理特性,易于区分。 Plasmodium falciparum lactate dehydrogenase (LDH-p) was isolated and purified from human erythrocyte LDH (LDH-r) and their characteristics were compared. The results showed that both nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide (NAD) could be promoted by LDH-p and LDH-r, and lactate and pyruvate could be transformed into each other. The same reaction was performed using the NAD analog, acetyl pyridine adenine dinucteotide (APAD), and LDH-r was unable to utilize APAD. In PAGE electrophoresis, NAD stained both LDH-p and LDH-r, the former being one band and the latter being three different bands. When APAD staining, only LDH-p was more stained and LDH-r band Neither color. The above shows that the two LDH have significantly different biochemical and physical properties, easy to distinguish.