Summary
Results with modified human red cell membrane sialoglycoproteins indicate that alkali-labile sialic acid and amino groups are parts of the erythrocyte receptor sites recognized by common rabbit and human anti-M and -N sera. The „N“ antigen, demonstrable in MM glycoprotein preparations by rabbit anti-N, has structural properties which are similar to those of the MN receptors. Sialic acid, amino groups and carbohydate, susceptible to periodate oxidation, are not involved in the Ss antigen sites. The specificity of theVicia graminea lectin is dependent on free amino and carboxyl groups. Its affinity for the substances is increased by blocking of amino groups.
Zusammenfassung
Untersuchungen mit modifizierten Sialoglykoproteinen aus menschlichen Erythrozyten zeigen, da\ alkali-labile NeuraminsÄure und Aminogruppen Bestandteile der Erythrozyten-Rezeptoren für gewöhnliche Anti-M und -N-Seren von Kaninchen und Menschen darstellen. Das „N“-Antigen, das durch Kaninchen Anti-N in MM-Glykoproteinpreparationen nachweisbar ist, hat Ähnliche strukturelle Eigenschaften wie die MN-Rezeptoren. Am Aufbau der Ss-Antigene sind NeuraminsÄure, durch Perjodat oxidierbares Kohlenhydrat und Aminogruppen nicht beteiligt. Die SpezifitÄt desVicia graminea Lektins hÄngt von freien Amino- und Carboxylgruppen ab. Seine AffinitÄt zu den Glykoproteinen wird durch Blockierung von Aminogruppen gesteigert.
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Herrn Prof. Dr. Peter Dahr zum 70. Geburtstag gewidmet.
Part of the work presented in this paper was first reported at the XIV Congress of the International Society of Blood Transfusion, Helsinki, July 27 to August 1, 1975.
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Uhlenbruck, G., Dahr, W., Schmalisch, R. et al. Studies on the receptors of the MNSs blood group system. Blut 32, 163–170 (1976). https://doi.org/10.1007/BF00995909
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DOI: https://doi.org/10.1007/BF00995909