Glycosylation of three molecular forms of human alpha1-acid glycoprotein having different interactions with concanavalin A. Variations in the occurrence of di-, tri-, and tetraantennary glycans and the degree of sialylation-Reference-Cited by-同舟云学术

Glycosylation of three molecular forms of human alpha1-acid glycoprotein having different interactions with concanavalin A. Variations in the occurrence of di-, tri-, and tetraantennary glycans and the degree of sialylation

Published:1988-08 Issue:2 Volume:175 Page:387-394
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

BIERHUIZEN Marti F. A.,WIT Moniek,GOVERS Carin A. R. L.,FERWERDA Wijnholt,KOELEMAN Carolien,POS Odette,DIJK Willem

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb14208.x/fullpdf

Reference30 articles.

1. Structure of α1-acid glycoprotein. Complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins

2. The carbohydrate units of human plasma α1-Acid glycoprotein

3. Evidence for uniformity of the carbohydrate chains in individual glycoprotein molecular variants

4. The use of concanavalin a crossed immuno-affinoelectrophoresis to detect hormone-associated variations in α1-acid glycoprotein

5. Evidence for alpha-1-acid glycoprotein populations of different pI values after concanavalin a affinity chromatography Study of their evolution during inflammation in man

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