Properties and characterization of binding protein dependent active transport of glutamine in isolated membrane vesicles of Escherichia coli.
Properties and characterization of binding protein dependent active transport of glutamine in isolated membrane vesicles of Escherichia coli.
复制标题
大肠杆菌分离膜囊泡中谷氨酰胺结合蛋白依赖性主动转运的特性和表征。
DOI：
10.1021/bi00273a021
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发表时间：
1983
期刊：
影响因子：
2.9
通讯作者：
Hong,J
中科院分区：
文献类型：
--
作者：
Hunt,AG;Hong,J
黄志刚，洪仁祥** *，黄志刚，等。大肠埃希菌膜囊中谷氨酰胺的活性转运[j] .生物工程学报。化学，256,11988-11991]。运输活性表现出相当窄的pH值，最佳pH值约为5.8，表观pKas为5.3和6.6，通过增加离子强度来抑制运输活性，并且需要钾和磷酸盐离子。然而，谷氨酰胺与谷氨酰胺结合蛋白的结合不受pH值在5-8范围内的影响，对高达1.0 Mkc1的离子强度变化相对不敏感，并且不需要钾和磷离子。由于囊泡的内部pH值在5-8范围内不会改变，因此pH依赖的转运谱很可能反映了配体谷氨酰胺结合蛋白与谷氨酰胺转运系统的膜结合组分的相互作用。
Arthur G. Hunt** and Jen-shiangHong* abstract: The reconstituted binding protein dependent active transport of glutamine in isolated membrane vesicles of Es-cherichia coli [Hunt, A. G., & Hong, J.(1981) J. Biol. Chem. 256, 11988-11991] is characterized in some detail. Transport activity exhibits a rather narrow pH optimum at about 5.8 with apparent pKas of 5.3 and 6.6, is inhibited by increasing ionic strength, and requires potassium and phosphate ions. How-ever, the binding of glutamine to the glutamine binding protein is unaffected by pH over a range of 5-8, is relatively insensitive to variation in ionic strength up to 1.0 Mkc1, and does not require potassium and phosphateions. Since the internal pH of vesicles does not change over the range of 5-8, the pH-dependent transport profile most probably reflects the interaction of liganded glutamine binding protein with the mem-brane-bound components of the glutamine transport system.