Effect of periodate oxidation on specific activities and carbohydrate components of human blood group N- and M-specific glycoproteins and glycopeptides.

Abstract:

: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 C8 and C1 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.

journal_name

Vox Sang

journal_title

Vox sanguinis

authors

Springer GF,Yang HJ

doi

10.1111/j.1423-0410.1978.tb02931.x

subject

Has Abstract

pub_date

1978-01-01 00:00:00

pages

255-64

issue

4

eissn

0042-9007

issn

1423-0410

journal_volume

35

pub_type

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