Hyper-heterogeneity of the N-terminus of recombinant BSF-2/IL-6 produced in CHO and NIH3T3 cells.
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.
Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.
N
N
Tonouchi
Y
Y
Miyasaka
H
H
Matsui
K
K
Miwa
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D004247:DNA / Q000235:genetics; D005784:Gene Amplification; D015850:Interleukin-6 / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008727:Methotrexate / Q000494:pharmacology; D051379:Mice; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D014162:Transfection
D015850:Interleukin-6; D011994:Recombinant Proteins; D004247:DNA; D008727:Methotrexate