两种部分纯化的钠离子依赖型氨基酸转运系统的特性研究。
The characterisation of two partially purified systems for Na+-dependent amino acid transport.
作者信息
Watts C, Wheeler K P
出版信息
Biochim Biophys Acta. 1980 Nov 4;602(2):446-59. doi: 10.1016/0005-2736(80)90323-5.
Two systems mediating the transport of amino acids were studied in vesicles derived from protein-depleted membranes of pigeon erythrocytes. One system (ASC system) catalysed the Na+-dependent exchange of small neutral amino acids, such as alanine, serine and cysteine. The other system, also Na+-dependent, mediated the active transport of glycine. The ASC and glycine systems were distinguished by the sensitivity of the latter to the anion present, by the former's requirement for an exchangeable amino acid and by the inability of alanine to inhibit the transport of glycine. Preliminary results indicated that the influx of glycine was electrically silent. The only major integral protein retained in the vesicles was the band 3 protein, but that could not be unequivocally identified as the transporter.
在源自鸽红细胞蛋白质缺乏膜的囊泡中研究了介导氨基酸转运的两个系统。一个系统（ASC系统）催化小中性氨基酸（如丙氨酸、丝氨酸和半胱氨酸）的Na⁺依赖性交换。另一个系统同样依赖Na⁺，介导甘氨酸的主动转运。ASC系统和甘氨酸系统的区别在于后者对存在的阴离子的敏感性、前者对可交换氨基酸的需求以及丙氨酸不能抑制甘氨酸的转运。初步结果表明甘氨酸的流入不产生电信号。囊泡中保留的唯一主要整合蛋白是带3蛋白，但无法明确将其鉴定为转运体。
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