Now showing items 1-10 of 100
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 ...
The human Aquaporin-5 gene. Molecular characterization and chromosomal localization.
(American Society for Biochemistry and Molecular Biology, 1996-04-12)
The cDNA for the fifth mammalian aquaporin (AQP5) was isolated from rat, and expression was demonstrated in rat salivary and lacrimal glands, cornea, and lung (Raina, S., Preston, G. M., Guggino, W. B., and Agre, P. (1995) ...
Quantification of Aquaporin-CHIP water channel protein in microdissected renal tubules by fluorescence-based ELISA
(American Society for Clinical Investigation, 1995-01)
Several transporters have been localized along the nephron by physiological methods or immunocytochemistry. However, the actual abundance of these molecules has not been established. To accomplish this goal, we have developed ...
Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements
(American Society for Clinical Investigation, 1990-08)
Protein 4.1 is an approximately 80-kD structural protein in the membrane skeleton which underlies and supports the erythrocyte plasma membrane. The preceding companion paper presents a biochemical study of two abnormal ...
The Rh polypeptide is a major fatty acid-acylated erythrocyte membrane protein
(American Society for Biochemistry and Molecular Biology, 1988-12-05)
The erythrocyte Rh antigens contain an Mr = 32,000 integral protein which is thought to contribute in some way to the organization of surrounding phospholipid. To search for possible fatty acid acylation of the Rh polypeptide, ...
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)
Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer silimar to channel proteins
(American Society for Biochemistry and Molecular Biology, 1991-04-05)
A novel Mr 28,000 erythrocyte transmembrane protein was recently purified and found to exist in two forms, "28kDa" and "gly28kDa," the latter containing N-linked carbohydrate (Denker, B. M., Smith, B. L., Kuhajda, F. P., ...
Heterotetrameric composition of aquaporin-4 water channels.
(American Chemical Society, 1999-08-24)
Aquaporin (AQP) water channel proteins are tetrameric assemblies of individually active approximately 30 kDa subunits. AQP4 is the predominant water channel protein in brain, but immunoblotting of native tissues has ...
Rapid gating and anion permeability of an intracellular aquaporin
(Nature Publishing Group, 1992-11-11)
Aquaporin (AQP) water-channel proteins are freely permeated by water but not by ions or charged solutes. Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular ...
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
(American Chemical Society, 1992)