Investigation of the structure and function of the human erythrocyte glucose transporter by proteolytic dissection

1987 ◽  
Vol 905 (2) ◽  
pp. 295-310 ◽  
Author(s):  
Michael T. Cairns ◽  
Javier Alvarez ◽  
Maria Panico ◽  
Angel F. Gibbs ◽  
Howard R. Morris ◽  
...  
1977 ◽  
Vol 165 (1) ◽  
pp. 157-161 ◽  
Author(s):  
M J A Tanner ◽  
D J Anstee ◽  
P A Judson

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.


2002 ◽  
Vol 277 (26) ◽  
pp. 23807-23814 ◽  
Author(s):  
Giovanna Valentini ◽  
Laurent R. Chiarelli ◽  
Riccardo Fortin ◽  
Manuela Dolzan ◽  
Alessandro Galizzi ◽  
...  

1986 ◽  
Vol 83 (8) ◽  
pp. 2652-2656 ◽  
Author(s):  
C. C. Chen ◽  
T. Kurokawa ◽  
S. Y. Shaw ◽  
L. G. Tillotson ◽  
S. Kalled ◽  
...  

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