Recombinant human erythropoietin: purification and analysis of carbohydrate linkage.

Abstract:

:Erythropoietin was purified to homogeneity from the culture medium of a baby hamster kidney cell line stably transfected with a human erythropoietin gene. A three-step procedure was used, which included affinity chromatography, ion-exchange chromatography, and reverse-phase chromatography. Purity of the protein was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino-terminal sequence analysis. Overall recovery was 35%. The biological activity of purified recombinant erythropoietin was similar to that of the native hormone in vitro. The purified recombinant hormone contained N-linked carbohydrate at residues 24, 38, and 83, and and O-linked carbohydrate at residue 126.

journal_name

Arch Biochem Biophys

authors

Broudy VC,Tait JF,Powell JS

doi

10.1016/0003-9861(88)90135-x

subject

Has Abstract

pub_date

1988-09-01 00:00:00

pages

329-36

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90135-X

journal_volume

265

pub_type

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