Midgley M
Biochem J. 1978 Jul 15;174(1):191-202. doi: 10.1042/bj1740191.
The transport of alpha-aminoisobutyrate into Crithidia fasciculata was characterized under aerobic and anaerobic conditions. Kinetic data for alpha-aminoisobutyrate transport were consistent with the operation of a single system of broad specificity that showed no marked dependence on Na+. Under anaerobic conditions alpha-aminoisobutyrate transport was inhibited by uncouplers such as 2,4-dinitrophenol, lipophilic cations such as methyltriphenylphosphonium ion and adenosine triphosphatase inhibitors such as dicyclohexylcarbodi-imide and NaN3. A working model in which alpha-aminoisobutyrate enters this organism by an H+-symport mechanism, the electrochemical gradient of protons being maintained by an H+-translocating adenosine triphosphatase on the cytoplasmic membrane, is proposed.
在需氧和厌氧条件下,对α-氨基异丁酸进入纤细短膜虫的转运过程进行了表征。α-氨基异丁酸转运的动力学数据与一个具有广泛特异性的单一系统的运作一致,该系统对钠离子没有明显依赖性。在厌氧条件下,α-氨基异丁酸的转运受到解偶联剂(如2,4-二硝基苯酚)、亲脂性阳离子(如甲基三苯基鏻离子)以及三磷酸腺苷酶抑制剂(如二环己基碳二亚胺和叠氮化钠)的抑制。提出了一个工作模型,其中α-氨基异丁酸通过H⁺共转运机制进入该生物体,质子的电化学梯度由细胞质膜上的H⁺转运三磷酸腺苷酶维持。