Cairney J, Higgins C F, Booth I R
J Bacteriol. 1984 Oct;160(1):22-7. doi: 10.1128/jb.160.1.22-27.1984.
Strains of Salmonella typhimurium deficient in one or more of the proline transport systems have been constructed and used to study the mechanism of energy coupling to transport. Proline uptake through the major proline permease (PP-I, putP) is shown to be absolutely coupled to Na+ ions and not to H+ ions as has previously been assumed. Transport through the minor proline permease (PP-II, proP), however, is unaffected by the presence or absence of Na+. The effect of Na+ on the kinetics of proline uptake shows that external Na+ increases the Vmax for transport. It seems probable that proline transport through PP-I is also coupled to Na+ ions in Escherichia coli.
已构建出鼠伤寒沙门氏菌中一种或多种脯氨酸转运系统缺陷的菌株,并用于研究能量与转运偶联的机制。通过主要脯氨酸通透酶(PP-I,putP)摄取脯氨酸被证明与Na⁺离子绝对偶联,而不像先前假设的那样与H⁺离子偶联。然而,通过次要脯氨酸通透酶(PP-II,proP)的转运不受Na⁺存在与否的影响。Na⁺对脯氨酸摄取动力学的影响表明,外部Na⁺增加了转运的Vmax。脯氨酸通过PP-I的转运在大肠杆菌中似乎也与Na⁺离子偶联。