| Literature DB >> 1603094 |
R C Grebenau1, D M Goldenberg, C H Chang, G A Koch, D V Gold, A Kunz, H J Hansen.
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 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.Entities:
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Year: 1992 PMID： 1603094 DOI： 10.1016/0161-5890(92)90185-z
Source DB: PubMed Journal: Mol Immunol ISSN： 0161-5890 Impact factor: 4.407