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)
Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
(National Academy of Sciences, 2005-02-08)
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
Temporary loss of perivascular aquaporin-4 in neocortex after transient middle cerebral artery occlusion in mice
(National Academy of Sciences, 2006-09-05)
The aquaporin-4 (AQP4) pool in the perivascular astrocyte membranes has been shown to be critically involved in the formation and dissolution of brain edema. Cerebral edema is a major cause of morbidity and mortality in ...
Molecular Cloning and Characterization of an Aquaporin cDNA from Salivary, Lacrimal, and Respiratory Tissues
(American Society for Biochemistry and Molecular Biology, 1995-01-27)
The Aquaporin family of water channels plays a fundamental role in transmembrane water movements in numerous plant and animal tissues. Since the molecular pathway by which water is secreted by salivary glands is unknown, ...
Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens
(American Society for Clinical Investigation, 1994-09)
Blood group antigens are structural variants in surface carbohydrate or amino acid polymorphisms on extracellular domains of membrane proteins. The red cell water channel-forming integral protein (Aquaporin CHIP) is a ...