Glycosylation pattern and disulfide assignments of recombinant human differentiation-stimulating factor.
This report describes the post-translational modifications of recombinant human differentiation-stimulating factor, a 180-residue glycoprotein that is secreted from transfected Chinese hamster ovary cells. Peptide peptides containing six potential N-glycosylation sites were analyzed to determine that Asn residues 9, 34, 63, 73, 96, and 116 were utilized. Additional peptides, generated by tryptic digestion of peptic fragments, allowed the assignments of three intrachain disulfide bonds (Cys-18 to Cys-131, Cys-12 to Cys-134, and Cys-60 to Cys-163).
Schmelzer
C H
CH
Department of Recovery Process Research and Development, Genentech, Inc., South San Francisco, California 94080.
Harris
R J
RJ
Butler
D
D
Yedinak
C M
CM
Wagner
K L
KL
Burton
L E
LE
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D003553:Cystine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D006031:Glycosylation; D006131:Growth Inhibitors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D015850:Interleukin-6; D053605:Leukemia Inhibitory Factor; D008222:Lymphokines / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D017421:Sequence Analysis
D004220:Disulfides; D006131:Growth Inhibitors; D015850:Interleukin-6; C507837:LIF protein, human; D053605:Leukemia Inhibitory Factor; D008222:Lymphokines; D010446:Peptide Fragments; D003553:Cystine