scholarly journals Studies on human red-cell membrane glycophorin A and glycophorin B genes in glycophorin-deficient individuals

1989 ◽  
Vol 263 (3) ◽  
pp. 993-996 ◽  
Author(s):  
C G Tate ◽  
M J A Tanner ◽  
P A Judson ◽  
D J Anstee

1. Genomic DNA derived from individuals who lack glycophorin A (GPA), glycophorin B (GPB) or both of these proteins was subjected to Southern-blot analysis using GPA and GPB cDNA probes. 2. Bands on the Southern blots were assigned to the GPA gene, GPB gene or to a putative pseudogene. 3. Genomic DNA derived from an individual of the Mk phenotype was shown to have deletions in the GPA and GPB genes. The simplest model for the results obtained is that a single deletion spans the GPA and GPB genes in the individual studied.

1980 ◽  
Vol 42 (1) ◽  
pp. 1-22 ◽  
Author(s):  
D. Litman ◽  
D.J. Hsu ◽  
V.T. Marchesi

Spectrin binds to a population of high-affinity sites on the exposed surface of inverted vesicles prepared from human red blood cell ghost membranes. Optimal spectrin binding requires the presence of monovalent salts but does not require calcium or magnesium. The band 2 subunit of spectrin, prepared in SDS, can also bind to vesicles, but isolated band 1 is inactive. Pre-incubation of inverted vesicles with antibodies directed against the cytoplasmic segment of band 3 or against bands 4.1-4.2 inhibits the binding of spectrin to the same vesicles. Antibodies against the cytoplasmic portion of glycophorin A have no effect. These results suggest that spectrin binds to a protein acceptor on the cytoplasmic surface of the red cell membrane which is close to the cytoplasmic segments of bands 3 and 4.1 and/or 4.2.


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