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Human fibroblastoid interferon: immunosorbent column chromatography and N-terminal amino acid sequence

1980/08/05 by H. Okamura, W. Berthold, Leroy Hood +4 · 2 citations
Biochemistry, Genetics and Molecular Biology · #Glycosylation and Glycoproteins Research #Proteoglycans and glycosaminoglycans research #Cancer, Hypoxia, and Metabolism

paper · doi:10.1021/bi00557a028

openalex publication_date 1980/08/05 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/11

Abstract

Three mice and one rabbit were inoculated with purified human fibroblastoid interferon. Neutralizing activity to human fibroblastoid interferon was observed in the serum of these animals with the rabbit showing the highest anti-interferon titers (10(6) neutralizing units/mL). Rabbit antiserum was coupled to cyanogen bromide activated Sepharose, and the resulting material was tested for use in the purification of human fibroblastoid interferon. Pure interferon obtained by this procedure was analyzed, and we report the sequence of the first 13 N-terminal amino acid residues of this protein.

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