Structure of the glycopeptides of a human gamma 1-immunoglobulin G (Tem) myeloma protein as determined by 360-megahertz nuclear magnetic resonance spectroscopy: Can.J.Biochem.

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TypeArticle
Journal titleCan.J.Biochem.
Volume60
Issue12
Pages11231131; # of pages: 9
SubjectALPHA; analysis; biantennary; cell; CELLS; chemistry; complex; COMPLEXES; FIELD; glycopeptide; Glycopeptides; Human; Immunoglobulin G; IMMUNOGLOBULIN-G; MAGNETIC; Magnetic Resonance Spectroscopy; MAGNETIC-RESONANCE; Myeloma Proteins; NUCLEAR; Nuclear Magnetic Resonance; nuclear magnetic resonance spectroscopy; NUCLEAR-MAGNETIC-RESONANCE; protein; Proteins; RESIDUES; RESONANCE; SPECTROSCOPY; structure; Support,Non-U.S.Gov't; transferase
AbstractHigh field magnetic resonance spectroscopy has been utilized to deduce the primary structure of the glycopeptides from a human myeloma gamma 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 alpha Man(1-6) and alpha Man(1-3) arms: (i) with beta Gal(1-4) and alpha NeuNAc(2-6), respectively (33%); (ii) with beta Gal(1-4) and beta Gal(1-4), respectively (45%); and (iii) beta Gal(1-4) and beta GlcNAc(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 beta GlcNAc(1-2) of the alpha Man(1-6) arm and that the sialyltransferase has a preference for the beta Gal(1-4) of the alpha Man(1-3) arm
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberGREY1982
NPARC number9372221
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Record identifierb1a2a56f-708f-42b7-97f3-38a5c8169bc6
Record created2009-07-10
Record modified2016-05-09
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