1. Biochemische Differenzierung der Pr1-/Pr2-determinierenden von der MN-determinierenden <em>N</em>-Acetyl-Neuraminsäure durch Acetylierungsversuche mit Erythrocytenglykoproteinen.
- Author
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Merz, Wolfgang and Roelcke, Dieter
- Subjects
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ERYTHROCYTES , *ANTIGENS , *IMMUNOGLOBULINS , *CHEMICAL reactions , *ACETIC acid , *FATTY acids , *PYRIDINE , *MANNOSE - Abstract
In contrast to MN receptors, Pr1 and Pr2 antigens of isolated glycoprotein of erythrocytes are not inactivated by acylation of free amino groups. By introduction of easily leaving groups, e.g. trifluoroacetic residues, inactivation of the MN activity can be made reversible. No differences between Pr1 and Pr2 antigens could be found with the reactions described in this paper. Acylation m aqueous phase (buffer/anhydrous acetic acid) and m organic phase (pyridine/ anhydrous acetic acid) gave identical results qualitatively and quantitatively. It was not possible to split the N-acetic binding neither under mild alkaline conditions nor with aminoacylase. 4-5 amino groups out of 11 could be acylated, whereas succinylation in aquous phase (buffer/ anhydrous succinic acid) resulted in modification of only one free amino group, the calculations being based on a molecular weight of 30 000. Following succinylation MN activity was also lost, whereas the antigenic activity of Pr1 and Pr2 remained unchanged. The appearance of a negative charge instead of the positive charge of the free amino group on the glycoprotein did not affect Pr1 or Pr2 activity m any way. If glycoprotein was esterified under conditions which cause esterification of free sialic acid to a wide extent neither MN activity nor Pr1/Pr2 activity was altered. [ABSTRACT FROM AUTHOR]
- Published
- 1971
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