Abstract
Analyses of glycosylation of the human monoclonal IgGl λ antibody (mab) CBGA1 are shown. The mab producing cell line was obtained by EBV transformation of peripheral blood lymphocytes of a healthy donor fused to the heteromyeloma CB-F7 (1). The human CBGA1 mab belongs to the multireactive group of natural antibodies, described as potential useful for treating bacteremic infections of gram negative bacteria as Pseudomonas aeruginosa, Klebsiella and E. coli (2). Two grams of mab were produced using suspension and hollow fibre bioreactors. The hollow fibre bioreactor was shown to be the most efficient system. Furthermore Fab- and Fc-fragments of the purified mab were prepared and analyzed. We found noteworthy heterogeneity of CBGA1 in SDS-PAGE and IEF. SDS-PAGE and lectinblot were used for glycosylation analysis. In addition to the N-glycosylation of the Fc part, a Fab fragment glycosylation could be shown. We found that both the VH and VL are glycosylated. The glycosylation pattern of the Fc fragment differs from that of the Fab. The VH-N-glycosylation site was located at position Asn 75 in frame III.
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