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Structural homology between glycophorins C and D of human erythrocytes.

Authors :
El-Maliki, Bouchra
Blanchard, Dominique
Dahr, Wolfgang
Beyreuther, Konrad
Cartron, Jean-Pierre
Source :
European Journal of Biochemistry; 8/15/89, Vol. 183 Issue 3, p639-643, 5p
Publication Year :
1989

Abstract

Glycophorin C (GPC) and D (GPD) are minor glycoproteins which are believed to be important for the structural integrity of the red cell membrane. We have investigated the structural relationship between these glycoproteins by both immunological and structural investigations: 1. A rabbit anti-serum produced against GPD reacts strongly with GPC and the abnormal glycoproteins of Gerbich: -2,-3 and Gerbich: -2,3 red cells, and recognizes most probably the homologous C-terminal portions of GPC and GPD. The two molecules however differ at their N-terminus. 2. One-dimensional mapping of the peptides obtained after tryptic, chymotryptic, V8 protease or acid cleavage of <superscript>125</superscript>I-labelled GPC and GPD, indicated that GPC and GPD are structurally related but some differences were found indicating that additional peptides were generated from GPC. 3. The partial primary structure of GPD was determined. The sequencing data are consistent with the assumption that GPD represents an abridged version of GPC that comprises residues approximately 21/29-128 and exhibits a N-terminal residue that is blocked by an as yet undefined group. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
183
Issue :
3
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
13790965
Full Text :
https://doi.org/10.1111/j.1432-1033.1989.tb21093.x