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Structure of the glycopeptides of a human γ 1 -immunoglobulin G (Tem) myeloma protein as determined by 360-megahertz nuclear magnetic resonance spectroscopy

1982; Canadian Science Publishing; Volume: 60; Issue: 12 Linguagem: Inglês

10.1139/o82-144

0008-4018

Arthur A. Grey, S Narasimhan, Jean Robert Brisson, Harry Schachter, J. P. Carver,

Monoclonal and Polyclonal Antibodies Research

High field magnetic resonance spectroscopy has been utilized to deduce the primary structure of the glycopeptides from a human myeloma γ 1 -immunoglobulin G (Tem). The major structures found belong to the biantennary complex class of glycopeptides, with a minor (5%) fraction belonging to the bisected biantennary complex class. In the biantennary class, three structures were present with different residues at the termini of the αMan(1-6) and αMan(1-3) arms: (i) with βGal(1-4) and αNeuNAc(2-6), respectively (33%); (ii) with βGal(1-4) and βGal(1-4), respectively (45%); and (iii) βGal(1-4) and βGlcNAc(1-2), respectively (17%). In the bisected biantennary class only the latter termini were found for the two arms. These results suggest that the galactosyl transferase in these cells has a preference for the βGlcNAc(1-2) of the αMan(1-6) arm and that the sialyltransferase has a preference for the βGal(1-4) of the αMan(1-3) arm.