人类肠道H⁺/寡肽共转运蛋白hPEPT1可转运具有相同电生性的不同电荷的二肽。
The human intestinal H+/oligopeptide cotransporter hPEPT1 transports differently-charged dipeptides with identical electrogenic properties.
作者信息
Mackenzie B, Fei Y J, Ganapathy V, Leibach F H
机构信息
Department of Physiology, UCLA School of Medicine 90095-1751, USA.
出版信息
Biochim Biophys Acta. 1996 Oct 23;1284(2):125-8. doi: 10.1016/s0005-2736(96)00170-8.
The human intestinal H+/oligopeptide cotransporter hPEPT1, expressed in Xenopus oocytes, transported neutral, anionic and cationic dipeptides with identical electrogenic properties and maximal evoked currents. Currents were activated by 1 H+ regardless of the net charge on the driven substrate, and were independent of Na+o, K+i and Clo-, calling into question the familiar concept of the origin of the transporter-mediated current.
在非洲爪蟾卵母细胞中表达的人类肠道H⁺/寡肽共转运体hPEPT1，以相同的电生性特性和最大诱发电流转运中性、阴离子和阳离子二肽。无论被转运底物上的净电荷如何，电流均由1个H⁺激活，且与细胞外Na⁺、细胞内K⁺和Cl⁻无关，这对转运体介导电流起源的传统概念提出了质疑。
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