Back to Search
Start Over
Structural analysis of the Ss sialoglycoprotein specific for Henshaw blood group from human erythrocyte membranes.
- Source :
- European Journal of Biochemistry; 5/15/84, Vol. 141 Issue 1, p51-55, 5p
- Publication Year :
- 1984
-
Abstract
- The N-terminal structures of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A, B) from two Henshaw (He) blood-group heterozygotes were determined by manual sequencing of tryptic glycopeptides and various secondary fragments. No structural alteration of the MN glycoprotein could be detected. The He-specific portion of the Ss glycoprotein was found to exhibit the N-terminal sequence Trp-...-...-...-Gly- (+ =glycosylation). Thus it differs at three positions from its normal counterpart which possesses 'N' activity and exhibits the N-terminal structure Leu-...-...-...-Glu-. Analysis of the Ss glycoprotein from 15 He-negative erythrocyte samples did not reveal any of the three He-specific structural alterations. The presence of a glycine residue at the fifth position of the blood-group-M-active MN glycoprotein as well as in the He-specific Ss glycoprotein provides an explanation for the occurrence of antisera (anti-M<superscript>e</superscript>) reacting with the M and He antigens. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 141
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 23563522
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1984.tb08155.x