Structure of the glycopeptides of a human γ1-immunoglobulin G (Tem) myeloma protein as determined by 360-megahertz nuclear magnetic resonance spectroscopy
- 30 November 1982
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 60 (12) , 1123-1131
- https://doi.org/10.1139/o82-144
Abstract
High field magnetic resonance spectroscopy was utilized to deduce the primary structure of the glycopeptides from a human myeloma .gamma.1-IgG (Tem). The major structures belong to the biatennary complex class of glycopeptides, with a minor (5%) fraction belonging to the bisected biantennary complex class. In the biantennary class, 3 structures were present with different residues at the termini of the .alpha.Man(1-6) and .alpha.Man(1-3) arms: with .beta.Gal(1-4) and .alpha.NeuNAc(2-6), respectively (33%); with .beta.Gal(1-4) and .beta.Gal(1-4), respectively (45%); and .beta.Gal(1-4) aGd .beta.GlcNAc(1-2), respectively (17%). In the bisected biantennary class only the latter termini were found for the 2 arms. The galactosyl transferase in these cells apparently has a preference for the .beta.GlcNAc(1-2) of the .alpha.Man(1-6) arm and the sialyltransferase apparently has a preference for the .beta.Gal(1-4) of the .alpha.Man(1-3) arm.Keywords
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