scholarly journals Separation and some properties of the major proteins of the human erythrocyte membrane

1972 ◽  
Vol 129 (2) ◽  
pp. 333-347 ◽  
Author(s):  
M. J. A. Tanner ◽  
D. H. Boxer
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Chemical Properties ◽  
Human Erythrocyte Membrane ◽  
Molecular Weights ◽  
Cell Surface Carbohydrate ◽  
Fractionation Procedure

A fractionation procedure is described which allows the isolation of three major human erythrocyte membrane proteins. Their isolation involves three sequential extraction procedures followed by gel filtration in 1% sodium dodecyl sulphate and preparative gel electrophoresis. All three proteins can be isolated from a single preparation. One of the proteins is the erythrocyte sialoglycoprotein, for which no C- or N-terminal residues were found. The other two proteins, which have not previously been isolated, have subunit molecular weights of 74000 and 93000 and contain 9 and 7% carbohydrate respectively. These glycoproteins have blocked N-terminal residues and show similarities in their chemical properties. Preparations derived from blood-group O erythrocytes contain no N-acetylgalactosamine, but similar preparations from blood-group A erythrocytes do contain this sugar. These three proteins cannot easily be solubilized by gentle aqueous procedures and represent about half of the erythrocyte ‘ghost’ protein. They carry a large proportion of the cell-surface carbohydrate.

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.

scholarly journals Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte

1980 ◽  
Vol 152 (1) ◽  
pp. 20-30 ◽  
Author(s):  
DT Fearon
Keyword(s):  
B Lymphocytes ◽  
Erythrocyte Membrane ◽  
Polymorphonuclear Leukocyte ◽  
Human Erythrocyte ◽  
B Lymphocyte ◽  
Sodium Dodecyl ◽  
Scatchard Analysis ◽  
Membrane Glycoprotein ◽  
Human Erythrocyte Membrane ◽  
C3b Receptor

A human erythrocyte membrane glycoprotein of 205,000 mol wt (gp205) has been identified as the C3b receptor of the erythrocyte, polymorphonuclear leukocyte (PMN), B lymphocyte, and monocyte. Initially, gp205 was sought and characterized as a constituent of the human erythrocyte membrane that can impair activation of the alternative complement pathway by inducing loss of function of the properdin-stabilized amplification C3 convertase (C3b,Bb,P) through displacement of Bb from C3b and by promoting cleavage-inactivation of C3b by C3b inactivator. These inhibitory activities of gp205 suggested that this membrane glyeoprotein had an affinity for C3b and prompted an analysis of its possible identity as the C3b receptor of human peripheral blood cells. The F(ab')2 fragment of rabbit IgG anti-gp205 inhibited the formation of rosettes with sheep EC3b of human erythroeytes, B lymphocytes, monocytes and PMN in a dose-response manner; the 50 percent inhibitory doses were 0.13/μg/ml, 0.90 μg/ml, 1.25 μg/ml, and 1.20 μg/ml of F(ab')2, respectively. Anti-gp205 did not impair the formation of rosettes by monocytes and B lymphocytes with sheep EC3bi or with EC3d. Scatchard analysis of the number of specific (125)I-F(ab')(2) anti-gp205 binding sites/cell revealed 950 sites/erythrocyte, 21,000 sites/cell of B lymphocyte preparation, 57,000 sites/PMN, and 48,000 sites/monocyte, indicating that the higher concentrations of antibody that had been required for inhibition of rosette formation by the nucleated cells reflected larger numbers of receptors on these cells. Direct evidence for the identity of gp205 as the C3b receptor of the four cell types was obtained when detergent-solubilized membrane proteins of the surface-radioiodinated cells were reacted with anti- gp205 and the immunoprecipitate was analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. In each instance, the antigenic material reacting with anti-gp205 represented a single protein with an apparent 205,000 mol wt. Thus, gp205 is the C3b receptor of human erythrocytes, PMN, B lymphocytes, and monocytes.

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
Sign in / Sign up

Export Citation Format

Share Document