Kayama-Gonda Y, Kawasaki T
J Bacteriol. 1979 Aug;139(2):560-4. doi: 10.1128/jb.139.2.560-564.1979.
Mechanisms of Li+ stimulation of proline transport were studied in cells of Escherichia coli 7 and NR70, a mutant of strain 7 lacking adenosine triphosphatase (EC 3.6.1.3). An electrochemical potential difference of Li+ induced in an inward direction of energy-depleted cells caused a transient uptake of proline depending on the driving force provided. When proline was added to unbuffered cell suspensions under anaerobic conditions, the medium was found to be acidified only in the presence of Li+ but not in the presence of Na+ or K+. This acidification was abolished by the addition of a permeant anion, SCN-, to the medium containing Li+, but this was not demonstrated with cells of a mutant strain deficient in a carrier protein specific for proline. These results support the assumption that proline is taken up by a mechanism of Li+-proline cotransport in E. coli.
在大肠杆菌7型和NR70(7型菌株的一个缺乏三磷酸腺苷酶(EC 3.6.1.3)的突变体)的细胞中研究了Li⁺刺激脯氨酸转运的机制。在能量耗尽的细胞中向内诱导的Li⁺电化学势差会导致脯氨酸的短暂摄取,这取决于所提供的驱动力。当在厌氧条件下将脯氨酸添加到未缓冲的细胞悬液中时,发现仅在存在Li⁺的情况下培养基会酸化,而在存在Na⁺或K⁺的情况下则不会。通过向含有Li⁺的培养基中添加渗透性阴离子SCN⁻可消除这种酸化,但对于缺乏脯氨酸特异性载体蛋白的突变菌株的细胞则未观察到这种情况。这些结果支持了大肠杆菌中脯氨酸通过Li⁺-脯氨酸共转运机制摄取的假设。