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首页> 外文期刊>Fiziologia: official journal of the Romanian Society of Physiological Sciences >Petition for the recognition of Gheorghe Benga as a discoverer of the first water channel protein in the human red blood cell membrane, several years before Peter Agre (2003 Nobel prize for chemistry)
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Petition for the recognition of Gheorghe Benga as a discoverer of the first water channel protein in the human red blood cell membrane, several years before Peter Agre (2003 Nobel prize for chemistry)

机译:承认Gheorghe Benga为人类红细胞膜中第一个水通道蛋白的发现者的请愿书,比Peter Agre(2003年诺贝尔化学奖)早了几年

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摘要

In 1986, Benga and coworkers (1) clearly demonstrated for the first time the presence and location of a water channel protein in the human red blood cell (RBC) membrane among polypeptides migrating in the region of 35-60 kDa on the electrophoretogram of RBC membranes, labeled with 203Hg-p-chloromercuribenzene sulfonate (PCMBS) under conditions for the specific inhibition of water diffusion. I suggested that a minor membrane component that binds PCMBS is involved in water transport and also indicated the way in which the specific protein could be further characterized: by purification and reconstitution in liposomes. In the same year the labeling experiments were confirmed and extended (2) and in the following 2-3 years I described the novelty of our work in several reviews (3-8). In 1988, Agre and coworkers purified a new protein from the RBC membrane (9), nick-named CHIP28 (channel-forming integral membrane protein of 28 kDa) (10). However, in addition to the 28 kDa component, the protein had a 35-60 kDa glycosylated component, i.e, the one we detected as the binding site of PCMBS under conditions for the inhibition of water transport across the RBC membrane (1,2). They suggested that CHIP28 may play a role in the linkage of the membrane skeleton to the lipid bilayer (9).
机译:1986年,Benga及其同事(1)首次清楚地证明了在RBC电泳图上以35-60 kDa的区域迁移的多肽中人红细胞(RBC)膜中水通道蛋白的存在和位置。膜,在特定抑制水扩散的条件下,用203Hg-对氯甲基水合苯磺酸盐(PCMBS)标记。我建议,与PCMBS结合的次要膜成分参与水的运输,并且还指出了可以进一步表征特定蛋白质的方式:通过脂质体的纯化和重建。同年,对标签实验进行了确认和扩展(2),在随后的2-3年中,我在几篇评论中描述了我们工作的新颖性(3-8)。 1988年,Agre及其同事从RBC膜中纯化了一种新蛋白(9),绰号为CHIP28(28 kDa的通道形成性整体膜蛋白)(10)。然而,除了28 kDa的成分外,该蛋白质还具有35-60 kDa的糖基化成分,即在抑制水通过RBC膜的条件下,我们检测到该成分为PCMBS的结合位点(1,2) 。他们认为CHIP28可能在膜骨架与脂质双层的连接中起作用(9)。

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