Molecular Basis of Tn‐Polyagglutinability1
- 1 July 1975
- journal article
- Published by Wiley in Vox Sanguinis
- Vol. 29 (1), 36-50
- https://doi.org/10.1111/j.1423-0410.1975.tb00475.x
Abstract
Spectrophotometric and gas-liquid chromatographic analyses on the carbohydrate moiety of tryptic erythrocyte glycopeptides from persons with Tn-syndrome reveal a selective lowering of the galactose and sialic acid content, the degree being dependent on the percentage of polyagglutinable cells. Alkaline borohydride specifically releases N-acetylgalactosaminitol, and the amount is correlated to the percentage of pathological acetylgalactosaminitol, and the amount is correlated to the percentage of pathological erythrocytes. It is concluded that the alkali-labile carbohydrate chains of Tn-polyagglutinable red cells solely consist of N-acetylgalactosamine linked to serine or threonine. Experiments with heterophile agglutinins whose specificity is known are in line with the above-mentioned results. As judged from SDS-polyacrylamide gel electrophoresis the three major membrane glycoproteins are affected to a different extent by the defect.Keywords
This publication has 40 references indexed in Scilit:
- Influence of Free Amino and Carboxyl Groups on the Specificity of Plant Anti-NVox Sanguinis, 1975
- Permanent Mixed‐Field Polyagglutinability (PMFP)Vox Sanguinis, 1973
- Antigénicité croisée des caséinoglycopeptides κ de vache et de brebis avec les antigenes des groupes sanguins M et NImmunochemistry, 1973
- Anti‐N Reagents in Elucidation of the Genetical Basis of Human Blood‐Group MN Specificities1Vox Sanguinis, 1972
- Human erythrocyte membrane glycoprotein: A re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresisBiochemical and Biophysical Research Communications, 1971
- Die Ficin-katalysierte Fragmentierung von Erythrozytenmembran-GlykoproteinenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1971
- Persistent Mixed Field PolyagglutinabilityVox Sanguinis, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Oligosaccharides from M-active sialoglycopeptides of human erythrocytesBiochemical and Biophysical Research Communications, 1969
- Studies of mucoproteins I. The structure of the prosthetic group of ovine submaxillary gland mucoproteinBiochimica et Biophysica Acta, 1959