Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation.

Abstract

A murine monoclonal anti-granulocyte IgG1, IMMU-MN3, was seen to exhibit heterogeneity. On reduced SDS-PAGE, the purified antibody appeared as two heavy-chain bands of unequal intensity, and only one light-chain band. Hydrophobic interaction chromatography (HIC) also resolved two populations of the IMMU-MN3 antibody. Based on Concanavalin A affinity… (More)

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Cite this paper

@article{Grebenau1992MicroheterogeneityOA, title={Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation.}, author={R C Grebenau and D. M. Goldenberg and C. H. Chang and Giacomo Koch and Dorothy Gold and Airton Kunz and H. J. Hansen}, journal={Molecular immunology}, year={1992}, volume={29 6}, pages={751-8} }