Erythrocyte Band 3 Protein e-book
by James M. Salhany
Erythrocyte Band Three Protein.
Erythrocyte Band Three Protein. Select Format: Hardcover. ISBN13:9780849368615.
Erythrocyte Band 3 Protein book.
Characterization of pyridoxal 5′-phosphate affinity labeling of band 3 protein. Evidence for allosterically interacting transport inhibitory subdomains. 262:15965–15973Google Scholar. Alterations in pyridoxal 5′-phosphate inhibition of human erythrocyte anion transport associated with osmotic hemolysis and resealing. 262:15,974–15,978Google Scholar. Erythrocyte Band 3 Protein, CRC, Boca Raton (FL)Google Scholar.
ISBN 10: 0849368618 ISBN 13: 9780849368615.
Deficiency of band 3 protein is found in a subset of HS patients who present with a phenotype of a mild to moderate . The oligosaccharide structures of the Ii-active band 3 proteins of erythrocytes from newborns and I adults are presented in Figure 13. Figure 13.
Deficiency of band 3 protein is found in a subset of HS patients who present with a phenotype of a mild to moderate dominantly inherited HS. Most, if not all, of these patients also have concomitant protein . deficiency. Numerous band 3 mutations associated with HS have been reported, spread throughout both the cytoplasmic and the membrane-spanning domains.
James M Salhany of The Nebraska Medical Center, Omaha . Band 3 Memphis variant II is a mutant anion-exchange protein associated with the Diego a+ blood group antigen.
James M Salhany of The Nebraska Medical Center, Omaha Read 107 publications Contact James M Salhany. Unanswered is whether miss-folding of band 3 during biosynthesis, or the absence of GPA modulation of properly folded band 3 is responsible.
Unilamellar vesicles of a diameter of 32 +/- 3 nm were then isolated from the sample by passage through a French press and subsequent gel filtration. According to sedimentation equilibrium measurements, around 85% of the vesicles were devoid of protein.
Affiliations: Biochemistry & Molecular Biology (2006) Band 3 (AE1, SLC4A1)-mediated transport of.
Affiliations: Biochemistry & Molecular Biology. University of Nebraska Medical Center, Omaha, NE, United States. Area: Erythrocyte Membrane Structure, Exchange & Hemolytic Anemia & Red Cell Homeostasis. Salhany JM. (2009) Kinetic evidence for modulation by glycophorin A of a conformational equilibrium between two states of band 3 (SLC4A1) bound reversibly by the competitive inhibitor DIDS. Blood Cells, Molecules & Diseases. 2006) Band 3 (AE1, SLC4A1)-mediated transport of. III: Role of solute and protein structure in proton-activated stilbenedisulfonate influx.
Anion transporters, binding proteins and senescent antigens. This book contains a collection of papers on the molecular biology of the band 3 proteins and their various functions: as anion transporters, binding proteins for membrane skeleton, hemoglobin and glycolytic enzymes, and as a recognition signal for the removal of senescent cells by the immuno-system of the body.
Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), is a protein that is encoded by the SLC4A1 gene in humans. Band 3 anion transport protein is a served transport protein responsible for mediating the exchange of chloride (Cl−) with bicarbonate (HCO3−) across plasma membranes. Functionally similar members of the AE clade are AE2 and AE3.