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

Abstract：

: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).

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Schmelzer CH,Harris RJ,Butler D,Yedinak CM,Wagner KL,Burton LE

doi

10.1006/abbi.1993.1243

subject

Has Abstract

pub_date

1993-05-01 00:00:00

pages

484-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(83)71243-9

journal_volume

302

pub_type

杂志文章

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