scholarly journals Abnormal minor human erythrocyte membrane sialoglycoprotein (β) in association with the rare blood-group antigen Webb (Wb)

1985 ◽  
Vol 232 (1) ◽  
pp. 289-291 ◽  
Author(s):  
M E Reid ◽  
M A Shaw ◽  
G Rowe ◽  
D J Anstee ◽  
M J Tanner
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Blood Group Antigen ◽  
Human Erythrocyte Membrane ◽  
Similar Treatment ◽  
Altered Form ◽  
Glycophorin C

Individuals whose erythrocytes are positive for the rare blood-group antigen Webb (Wb) have an altered form of the minor sialoglycoprotein beta (synonyms glycophorin C and glycoconnectin). This altered sialoglycoprotein beta (beta Wb) has an Mr about 2700 lower than that of normal sialoglycoprotein beta. Treatment of normal sialoglycoprotein beta with endo-beta-N-acetylglucosaminidase F decreased its Mr by about 3600, but similar treatment of sialoglycoprotein beta Wb had no effect. These results suggest the possibility that sialoglycoprotein beta Wb lacks the N-glycosidically linked oligosaccharide found on normal sialoglycoprotein beta.

scholarly journals Structural relationships between human erythrocyte sialoglycoproteins β and γ and abnormal sialoglycoproteins found in certain rare human erythrocyte variants lacking the Gerbich blood-group antigen(s)

1987 ◽  
Vol 244 (1) ◽  
pp. 123-128 ◽  
Author(s):  
M E Reid ◽  
D J Anstee ◽  
M J A Tanner ◽  
K Ridgwell ◽  
G T Nurse
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Blood Group Antigen ◽  
Human Erythrocyte Membrane ◽  
Diffuse Band ◽  
Structural Relationships ◽  
Normal Erythrocyte

The human erythrocyte membrane sialoglycoproteins beta and gamma are important for the maintenance of the discoid shape of the normal erythrocyte. In this paper we show that the human erythrocyte sialoglycoproteins beta and gamma (hereafter called beta and gamma) are structurally related. Rabbit antisera produced against purified beta and beta 1 and rendered specific to the cytoplasmic portion of these proteins also react with the cytoplasmic portion of gamma. Some human anti-Gerbich (Ge) sera react with the extracellular portion of both beta and gamma. This reactivity is shown to be directed towards a common epitope on beta and gamma. However, most anti-Ge sera do not react with beta, but react with an extracellular epitope only present on gamma. All individuals who lack the Ge antigens lack beta and gamma. In some cases abnormal sialoglycoproteins are present in the erythrocytes, and these are shown to be structurally related to beta and gamma. Rabbit antisera raised against the purified abnormal sialoglycoprotein from a Ge-negative erythrocyte type reacted with the cytoplasmic portion of both beta and gamma. Unlike normal beta and gamma, the abnormal sialoglycoproteins found in Ge-negative erythrocytes migrate as a diffuse band on SDS/polyacrylamide-gel electrophoresis. Studies using endoglycosidases suggest that the diffuse nature of these bands results from carbohydrate heterogeneity and that the abnormal sialoglycoproteins contain N-glycosidically linked oligosaccharides with repeating lactosamine units. Such polylactosamine chains are not present on normal beta or gamma.

High Frequency Antigens of Human Erythrocyte Membrane Sialoglycoproteins, V.Characterization of the Gerbich Blood Group Antigens: Ge2 and Ge3

1987 ◽  
Vol 368 (2) ◽  
pp. 1375-1384 ◽  
Author(s):  
Wolfgang DAHR ◽  
Siegrid KIEDROWSKI ◽  
Dominique BLANCHARD ◽  
Patricia HERMAND ◽  
John J. MOULDS ◽  
...  
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
High Frequency ◽  
Blood Group Antigens ◽  
Human Erythrocyte Membrane
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