Biochemische Differenzierung der Pr1‐/Pr2‐determinierenden von der MN‐determinierenden N‐Acetyl‐Neuraminsäure durch Acetylierungsversuche mit Erythrocytenglykoproteinen

摘要: In contrast to MN receptors, Pr1 and Pr2 antigens of isolated glycoprotein erythrocytes are not inactivated by acylation free amino groups. By introduction easily leaving groups, e.g. trifluoroactic residues, inactivation the activity can be made reversible. No differences between could found with reactions described in this paper. Acylation aqueous phase (buffer/anhydrous acetic acid) organic (pyridine/anhydrous gave identical results qualitatively quantitatively. It was possible split N-acetic binding neither under mild alkaline conditions nor aminoacylase. 4–5 groups out 11 acylated, whereas succinylation aquous succinic resulted modification only one group, calculations being based on a molecular weight 30000. Following also lost, antigenic remained unchanged. The appearance negative charge instead positive group did affect or any way. If esterified which cause esterification sialic acid wide extent Pr1/Pr2 altered.