Hansen B D, Webster H K, Hendricks L D, Pappas M G
Exp Parasitol. 1984 Aug;58(1):101-9. doi: 10.1016/0014-4894(84)90025-0.
Leishmania mexicana mexicana promastigotes, axenic amastigotes, and amastigotes derived from Vero cells were examined for de novo purine synthesis and mechanisms of purine salvage. Both promastigotes and axenic amastigotes were incapable of de novo purine synthesis, as shown by the lack of [14C]formate and [14C]glycine incorporation into purine nucleotide pools. However, the ready incorporation of [14C]hypoxanthine, [14C]adenine, and [14C]guanine suggested that purine salvage pathways were operating. In addition, a significant percentage (greater than or equal to 60%) of the total label from these purine precursors was associated with adenylate nucleotides. Nucleotide pool levels of axenic amastigotes were consistently greater but the specific activities were less than those of promastigotes, suggesting a slower rate of purine metabolism in the axenic amastigote form. Similar results were obtained from amastigotes isolated from infected Vero cells.
对墨西哥利什曼原虫墨西哥亚种前鞭毛体、无共生体无鞭毛体以及源自非洲绿猴肾细胞(Vero细胞)的无鞭毛体进行了嘌呤从头合成和嘌呤补救机制的检测。前鞭毛体和无共生体无鞭毛体均无法进行嘌呤从头合成,这表现为[¹⁴C]甲酸和[¹⁴C]甘氨酸未掺入嘌呤核苷酸库。然而,[¹⁴C]次黄嘌呤、[¹⁴C]腺嘌呤和[¹⁴C]鸟嘌呤易于掺入,这表明嘌呤补救途径在起作用。此外,这些嘌呤前体的总标记中有相当大比例(大于或等于60%)与腺苷酸核苷酸相关。无共生体无鞭毛体的核苷酸库水平始终更高,但比活性低于前鞭毛体,这表明无共生体无鞭毛体形式的嘌呤代谢速率较慢。从感染的Vero细胞中分离出的无鞭毛体也得到了类似结果。