Uniformity of Glycans within Molecular Variants of αl‐Protease Inhibitor with Distinct Affinity for Concanavalin A
- 1 May 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 124 (2) , 371-376
- https://doi.org/10.1111/j.1432-1033.1982.tb06602.x
Abstract
Human .alpha.1-protease inhibitor contains 4 asparagine-linked carbohydrate chains/molecule. Three types of carbohydrate chains were released from the polypeptide backbone by hydrazinolysis: (a) biantennary (80%), (b) biantennary with an intercalated N-acetylglucosamine residue (14%), and (c) triantennary (6%). Using concanavalin-A-affinity chromatography, native and S-carboxymethylated .alpha.1-protease inhibitor were fractionated into 3 distinct molecular variants which were shown to contain only one type (a, b or c, respectively), of glycan/molecule. This and previous observations on other serum glycoproteins support the proposal of uniformity of glycan type within individual molecular variants of glycoproteins.This publication has 34 references indexed in Scilit:
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