Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Glycosylation pattern and disulfide assignments of recombinant human differentiation-stimulating factor.

Schmelzer C.H., Harris R.J., Butler D., Yedinak C.M., Wagner K.L., Burton L.E.

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).

Arch. Biochem. Biophys. 302:484-489(1993) [PubMed] [Europe PMC]

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again