Recombinant human fibrinogen and sulfation of the γ′ chain

David Farrell, Eileen R. Mulvihill, Shaoming Huang, Dominic W. Chung, Earl W. Davie

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Abstract

Human fibrinogen and the homodimeric γ′-chain-containing variant have been expressed in BHK cells using cDNAs coding for the α, β, and γ (or γ′) chains. The fibrinogens were secreted at levels greater than 4 μg (mg of total cell protein)-1 day-1 and were biologically active in clotting assays. Recombinant fibrinogen containing the γ′ chain incorporated 35SO4 into its chains during biosynthesis, while no incorporation occurred in the protein containing the γ chain. The identity of the sulfated γ′ chain was verified by its ability to form dimers during clotting. In addition, carboxypeptidase Y digestion of the recombinant fibrinogen containing the γ′ chain released 96% of the 35S label from the sulfated chain, and the radioactive material was identified as tyrosine O-sulfate. These results clarify previous findings of the sulfation of tyrosine in human fibrinogen.

Original languageEnglish (US)
Pages (from-to)9414-9420
Number of pages7
JournalBiochemistry
Volume30
Issue number39
Publication statusPublished - 1991
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Farrell, D., Mulvihill, E. R., Huang, S., Chung, D. W., & Davie, E. W. (1991). Recombinant human fibrinogen and sulfation of the γ′ chain. Biochemistry, 30(39), 9414-9420.