Format

Send to

Choose Destination
J Chromatogr. 1988 Nov 11;454:205-15.

Structural characterization of recombinant consensus interferon-alpha.

Author information

1
Amgen Inc., Thousand Oaks, CA 91320.

Abstract

Recombinant consensus interferon-alpha is derived from genetically modified Escherichia coli containing a synthetic gene constructed from a consensus of interferon sequences. The purified and biologically active protein has been subjected to detailed structural characterization including sequence determination and peptide isolation and identification. The homogeneous consensus interferon-alpha preparation contains two chromatographically indistinguishable homologous polypeptides with one containing an extra methionyl residue at the amino terminus. The delineated amino acid sequence of the protein is identical to that expected from the coding sequence of the gene. Correct oxidation of the molecule has been confirmed with two intramolecular disulfide linkages observed at Cys(1)-Cys(99) and Cys(29)-Cys(139).

PMID:
3235597
DOI:
10.1016/s0021-9673(00)88614-8
[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center