Partial Purification of ABO Blood Group Antigens: Sodium Deoxycholate Fractionation of Human Erythrocyte Membranes

Vox Sanguinis ◽  
1974 ◽  
Vol 27 (6) ◽  
pp. 504-514 ◽  
Author(s):  
Steven H. Zuckerman ◽  
Stanley C. Uretsky ◽  
Steven D. Douglas
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Sodium Deoxycholate ◽  
Erythrocyte Membranes ◽  
Partial Purification ◽  
Abo Blood Group ◽  
Blood Group Antigens ◽  
Human Erythrocyte Membranes

scholarly journals Release of Oligosaccharides from Human Erythrocyte Membranes of Different Blood-Group-P Phenotypes by Trifluoroacetolysis

1980 ◽  
Vol 104 (2) ◽  
pp. 323-330 ◽  
Author(s):  
Arne LUNDBLAD ◽  
Sigfrid SVENSSON ◽  
Bengt LOW ◽  
Lisbeth MESSETER ◽  
Bertil CEDERGREN
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes ◽  
Blood Group P

scholarly journals A carbohydrate-deficient membrane glycoprotein in human erythrocytes of phenotype S-s-

1977 ◽  
Vol 165 (1) ◽  
pp. 157-161 ◽  
Author(s):  
M J A Tanner ◽  
D J Anstee ◽  
P A Judson
Keyword(s):  
Blood Group ◽  
Arachis Hypogaea ◽  
Human Erythrocyte ◽  
Structure And Function ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Membrane Glycoprotein ◽  
Blood Group Antigens ◽  
And Function ◽  
Normal Erythrocyte

1. We investigated the membranes of human erythrocytes which completely lack the blood-group antigens S and s (denoted as S-s-) as part of a study of the structure and function of the surface glycoproteins of the human erythrocyte. 2. The S-s-erythrocyte-membrane glycoprotein PAS-3 band was much less intensely stained in comparison with that of the glycoprotein from normal erythrocyte membranes. The S-s-membrane glycoprotein PAS-4 band also showed decreased staining. 3. Examination with the lectins from Maclura aurantiaca (Osage orange) and Arachis hypogaea (groundnut) showed that the PAS-3 glycoprotein of S-s-erythrocyte membranes lacked the receptors for these lectins that are present on glycoprotein PAS-3 from normal erythrocytes. 4. Radioiodination with lactoperoxidase showed the presence of the polypeptide of glycoprotein PAS-3 in S-s-cells, although it was more weakly labelled than the protein in the normal erythrocyte. 5. Our results show that the PAS-3 glycoprotein of S-s-erythrocytes is deficient in some of the carbohydrates present in the protein from normal erythrocytes. Glycoprotein PAS-4 of normal erythrocytes is shown to be a complex containing both glycoproteins PAS-1 and PAS-3.

Solubilized Glycoprotein from Human Erythrocyte Membranes Possessing Blood Group A, B and H Activity

Vox Sanguinis ◽  
1969 ◽  
Vol 17 (4) ◽  
pp. 289-299 ◽  
Author(s):  
N. B. Whittemore ◽  
N. C. Trabold ◽  
C. F. Reed ◽  
R. I. Weed
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Blood Group A ◽  
Human Erythrocyte Membranes ◽  
Group A

scholarly journals Structural analysis of the Ss sialoglycoprotein specific for Henshaw blood group from human erythrocyte membranes

1984 ◽  
Vol 141 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Wolfgang DAHR ◽  
Maria KORDOWICZ ◽  
W. John JUDD ◽  
John MOULDS ◽  
Konrad BEYREUTHER ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

Immunopurification of the blood group RhD protein from human erythrocyte membranes

1999 ◽  
Vol 735 (2) ◽  
pp. 207-217 ◽  
Author(s):  
Sylvie Cochet ◽  
Antoine Blancher ◽  
Francis Roubinet ◽  
Claude Hattab ◽  
Jean-Pierre Cartron ◽  
...  
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

Ss blood Group Associated PAS-staining polymorphism of glycoprotein 3 from human erythrocyte membranes

1976 ◽  
Vol 32 (2) ◽  
pp. 121-132 ◽  
Author(s):  
W. Dahr ◽  
G. Uhlenbruck ◽  
R. Schmalisch ◽  
E. Jan�en
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes ◽  
Pas Staining

scholarly journals Blood-group-Ii-active gangliosides of human erythrocyte membranes

1978 ◽  
Vol 173 (1) ◽  
pp. 245-254 ◽  
Author(s):  
T Feizi ◽  
R A Childs ◽  
S I Hakomori ◽  
M E Powell
Keyword(s):  
Blood Group ◽  
Silica Gel ◽  
Human Erythrocyte ◽  
Porous Silica ◽  
Erythrocyte Membranes ◽  
Group I ◽  
Internal Structures ◽  
Human Erythrocyte Membranes ◽  
Porous Silica Gel ◽  
Group Ii

More than ten new types of gangliosides, in addition to haematoside and sialosylparagloboside, were isolated from human erythrocyte membranes. These were separated by successive chromatographies on DEAE-Sephadex, on porous silica-gel columns and on thin-layer silica gel as acetylated compounds. Highly potent blood-group-Ii and moderate blood-group-H activities were demonstrated in some of the ganglioside fractions. The gangliosides incorporated into cholesterol/phosphatidylcholine liposomes stoicheiometrically inhibited binding of anti-(blood-group I and i) antibodies to a radioiodinated blood-group-Ii-active glycoprotein. The fraction with the highest blood-group-I-activity, I(g) fraction, behaved like sialosyl-deca- to -dodeca-glycosylceramides on t.l.c. Certain blood-group-I and most of the -i determinants were in partially or completely cryptic form and could be unmasked by sialidase treatment. Thus the I and i antigens, which are known to occur on internal structures of blood-group-ABH-active glycoproteins in secretions, also occur in the interior of the carbohydrate chains of erythrocyte gangliosides.

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