2. Academic Validation
  3. Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation

Microheterogeneity of a purified IgG1 due to asymmetric Fab glycosylation

  • Mol Immunol. 1992 Jun;29(6):751-8. doi: 10.1016/0161-5890(92)90185-z.
R C Grebenau 1,  D M Goldenberg,  C H Chang,  G A Koch,  D V Gold,  A Kunz,  H J Hansen
Affiliations

Affiliation

  • 1 Immunomedics Inc., Newark, NJ 07103.
PMID: 1603094 DOI: 10.1016/0161-5890(92)90185-z
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.

Figures
Products