Results 211 to 220 of about 21,169,060 (256)
Some of the next articles are maybe not open access.
Transfusion Medicine, 1997
Glycophorin C (GPC) and glycophorin D (GPD) are closely related sialoglycoproteins in the human red blood cell (RBC) membrane. Both are thought to be encoded by the GPC gene (GYPC). We report here the new GPC variant, MAT, with a high‐molecular‐weight form of GPC and GPD.
M, Uchikawa +4 more
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Glycophorin C (GPC) and glycophorin D (GPD) are closely related sialoglycoproteins in the human red blood cell (RBC) membrane. Both are thought to be encoded by the GPC gene (GYPC). We report here the new GPC variant, MAT, with a high‐molecular‐weight form of GPC and GPD.
M, Uchikawa +4 more
openaire +2 more sources
Blood, 2001
AbstractBand 3 and glycophorin A (GPA) are the 2 most abundant integral proteins in the human erythrocyte membrane. Earlier studies suggested that the 2 proteins may associate not only in the mature erythrocyte membrane, but also during their posttranslational processing and intracellular trafficking.
I, Auffray +8 more
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AbstractBand 3 and glycophorin A (GPA) are the 2 most abundant integral proteins in the human erythrocyte membrane. Earlier studies suggested that the 2 proteins may associate not only in the mature erythrocyte membrane, but also during their posttranslational processing and intracellular trafficking.
I, Auffray +8 more
openaire +2 more sources
Monoclonal antibodies to cyanogen bromide fragments of glycophorin A
Molecular Immunology, 1985Eleven mouse monoclonal antibodies directed against epitopes on CNBr peptides of the major sialoglycoconjugate of the human red blood cell, glycophorin A, have been produced by hybridomas derived from P3-X63-Ag8.653 myeloma cells and spleen cells from BALB/c mice immunized with purified glycophorin.
A L, Barsoum +2 more
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Modification of glycophorin A during oxidation of erythrocyte membrane
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1990Human erythrocyte ghosts were oxidized with tert-butyl hydroperoxide and subsequently treated with tritiated borohydride to label the membrane proteins modified during the membrane oxidation. From the ghosts, oxidized-and-tritiated glycophorin A was isolated and characterized.
M, Beppu +4 more
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Molecular Immunology, 1985
A new hemagglutinating monoclonal antibody, MoAb31, detected glycophorins A and B in Western blots. Results with enzyme-modified erythrocytes indicated the MoAb31 determinants were sialic acid dependent, and resided on glycophorin A on the trypsin-resistant, ficin-sensitive segment, and on glycophorin B on the ficin-sensitive segment.
A, Rearden +4 more
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A new hemagglutinating monoclonal antibody, MoAb31, detected glycophorins A and B in Western blots. Results with enzyme-modified erythrocytes indicated the MoAb31 determinants were sialic acid dependent, and resided on glycophorin A on the trypsin-resistant, ficin-sensitive segment, and on glycophorin B on the ficin-sensitive segment.
A, Rearden +4 more
openaire +2 more sources
Red cell antigens on band 3 and glycophorin A
Blood Reviews, 2000Band 3 and glycophorin A (GPA) are the two most abundant integral proteins of the red cell membrane, being present in approximately 10(6) copies per cell. The main functions of band 3 are membrane anion transport and maintenance of red cell membrane stability through interaction with the cytoskeleton.
openaire +2 more sources
Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase.
Journal of the American Chemical Society, 2015R. Trenker, M. Call, M. J. Call
semanticscholar +1 more source
American Journal of Surgical Pathology, 2011
H. Dong, S. Wilkes, Haisu Yang
semanticscholar +1 more source
H. Dong, S. Wilkes, Haisu Yang
semanticscholar +1 more source

