Abstract
In 1986, Benga and coworkers 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 kD on the electrophoretogram of RBC membranes, labeled with [203]Hg-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, and in the following 2-3 years I described the novelty of our work in several reviews. Biomedical Reviews 2006; 17: ix-xi.
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