Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation
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...
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Published in | Molecular immunology Vol. 29; no. 6; p. 751 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
01.06.1992
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Subjects | |
Online Access | Get more information |
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Summary: | 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 chromatography, enzymatic digestion with Endoglycosidase F and carbohydrate analysis, it was found that the heterogeneity detected by SDS-PAGE and HIC was due to differences in glycosylation. Furthermore, sequential gel analysis (non-reduced/reduced) demonstrated that the upper heavy-chain band was asymmetrically glycosylated. |
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ISSN: | 0161-5890 |
DOI: | 10.1016/0161-5890(92)90185-Z |