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Effect of Periodate Oxidation on Specific Activities and Carbohydrate Components of Human Blood Group N‐ and M‐Specific Glycoproteins and Glycopeptides 1
Author(s) -
Springer G. F.,
Yang H. J.
Publication year - 1978
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1978.tb02931.x
Subject(s) - glycopeptide , periodate , glycoprotein , antiserum , chemistry , biochemistry , carbohydrate , periodic acid , galactose , antibody , biology , immunology , antibiotics
. Mild as well as strong periodate oxidation of isolated erythrocyte N and M glycoproteins and glycopeptides gave extensive to complete destruction of N‐specificities as measured with Vicia graminea extracts and of N‐ as well as M‐ activities determined with all but 1 of 8 animal anti‐N and 13 anti‐M sera. Results with human antisera differed somewhat, while the specificity of mildly oxidized N‐glycoprotein was completely destroyed as determined with all 8 human anti‐N sera used, that of strongly oxidized N‐active substance was completely inactivated towards one of the human antisera; the remainder showed 63–94% destruction, and 2 sera indicated no effect of oxidation. Similarly, while 10 of 14 human anti‐M indicated complete inactivation of M‐specific glycoproteins and glycopeptides after mild or strong oxidation, 2 showed partial inactivation and 2 human anti‐M sera showed no inactivating effect of oxidation. The most relevant findings of quantitative carbohydrate analysis of periodate oxidized N‐ and M‐specific substance were extensive transformation of N‐acetylneuraminic acid (NAN) to its C 8 and C 1 analogues on mild oxidation and pronounced destruction of NAN and its analogues on strong oxidation; however, some intact NAN always remained. In all instances galactose (Gal) was destroyed to a much larger extent in N‐derived than in M‐derived glycoproteins and glycopeptides.