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Recombinant human BSF-2 (B cell stimulatory factor 2/Interleukin 6; IL-6) proteins were purified from CHO and NIH3T3 cell cultures and characterized. The lectin binding patterns suggested that the proteins have N-linked oligosaccharide(s) with tri-antennary structure of bisecting GlcNAc. Their N-termini were highly heterogeneous; at least five closely related N-termini were detected. This N-terminal heterogeneity was not generated in the cell culture because no processing activity was found in the culture medium.

Hyper-heterogeneity of the N-terminus of recombinant BSF-2/IL-6 produced in CHO and NIH3T3 cells.