Now showing items 1-6 of 6
Association between human erythrocyte calmodulin and the cytoplasmic surface of human erythrocyte membranes
(American Society for Biochemistry and Molecular Biology, 1983-05-25)
This report describes Ca2+-dependent binding of 125I-labeled calmodulin (125I-CaM) to erythrocyte membranes and identification of two new CaM-binding proteins. Erythrocyte CaM labeled with 125I-Bolton Hunter reagent fully ...
Concurrent expression of erythroid and renal aquaporin CHIP and appearance of water channel activity in perinatal rats
(American Society for Clinical Investigation, 1993-10)
Major phenotypic changes occur in red cell membranes during the perinatal period, but the underlying molecular explanations remain poorly defined. Aquaporin CHIP, the major erythroid and renal water channel, was studied ...
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992)
Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein
(American Association for the Advancement of Science, 1992-04-17)
Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is ...
Mammalian red cell membrane Rh polypeptides are selectively palmitoylated subunits of a macromolecular complex
(American Society for Biochemistry and Molecular Biology, 1992-03-15)
Incubation of [3H]palmitic acid, ATP, and CoA with inside-out membrane vesicles prepared from human or other mammalian red cells resulted in nearly exclusive 3H-palmitoylation of the Mr = 32,000 Rh polypeptides. [3H]Palmitic, ...
Biologically active two-dimensional crystals of aquaporin CHIP
(American Society for Biochemistry and Molecular Biology, 1994-01-21)
Plasma membranes of several mammalian tissues are highly permeable to water due to the presence of CHIP, the 28-kDa channel-forming integral protein which is the archetypal member of the aquaporin family of water channel ...