The isolation and amino acid/sugar composition of human fibroblastoid interferon.

Tan, Y. H.; Barakat, Fatima; Berthold, Wolfgang; Smith-Johannsen, Heidi; Tan, Celine

doi:10.1016/s0021-9258(18)36051-4

Cited by 69 publications

(13 citation statements)

References 20 publications

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“…Mature MuIFN-a2 is encoded by 167 amino acids, the additional amino acid being the carboxy terminal one, probably due to an insertion of three nucleoticLes just before the termination triplet. There is a potential glycosylation peptide sequence Asn-Ala-Thr at positions 78-80. i1uIFN-3, which is thought to be glycosylated (15)(16)(17), but not human alpha IFNs, also have a potential glycosylation sequence in this position.…”

Section: Discussionmentioning

confidence: 99%

Structure and expression of cloned murine IFN-α genes

Shaw¹,

Boll²,

Taira³

et al. 1983

Nucl Acids Res

154

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The mouse has an interferon-alpha (MuIFN-alpha) gene family containing at least four, and likely more than ten members. A segment of mouse chromosomal DNA and cDNAs encoding murine alpha IFNs have been cloned, and the sequence of two MuIFN-alpha DNAs determined. No intron was found in the chromosomal gene. The two coding sequences produced biologically active IFN when expressed in monkey cells under the control of an SV40 promoter, and in E.coli under the control of the ampicillinase promoter. MuIFN-alpha 1 had no detectable activity on human cells, while MuIFN-alpha 2 was 20% as active on human as on mouse cells.

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Section: Discussionmentioning

confidence: 99%

Structure and expression of cloned murine IFN-α genes

Shaw¹,

Boll²,

Taira³

et al. 1983

Nucl Acids Res

154

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“…Interferon Production and Assay. Interferon was produced and concentrated from a C-10 cell line as previously described in serum-containing or serum-free medium (Tan et al, 1979) 0006-2960/80/0419-3831$01.00/0 tiserum 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.…”

Section: Methodsmentioning

confidence: 99%

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

Okamura¹,

Berthold²,

Hood³

et al. 1980

Biochemistry

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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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“…It has been stabilized by the addition of detergents, carrier proteins such as human serum albumin, antioxidants or rare-earth salts (Sedmak & Grossberg 1979). Amino acid analyses confirmed that IFN-p is a highly hydrophobic protein (Tan 1979;Knight et al 1980;Friesen et al 1981). Four lines of evidence indicate that fibroblast interferon is a glycoprotein.…”

Section: (B) Human Fibroblast Interferonmentioning

confidence: 99%

“…Four lines of evidence indicate that fibroblast interferon is a glycoprotein. It binds to Con A-Sepharose and can be eluted specifically by a-methyl mannoside (Davey et al 1976); pure IFN-p can be stained on polyacrylamide gel by Schiff base (Knight 1976); amino sugar analysis has detected several residues of glucosamine (Tan et al 1979;Friesen et al 1981); finally, a glycosylation signal sequence Asn-Asp-Ser was found in positions 72-74 of mature IFN-p.…”

Section: (B) Human Fibroblast Interferonmentioning

confidence: 99%

Purification and structural analysis of interferon

Rubinstein

1982

Phil. Trans. R. Soc. Lond. B

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Studies with crude or partly purified interferon have provided a significant amount of structural information. However, complete biochemical characterization required purification to homogeneity. Earlier work on fractionation has met with many difficulties because interferon was available only in minute quantities. A scale-up of production, adaptation of multi-step purification schemes, use of high-resolution separation techniques and highly sensitive analytical methods have yielded pure interferons and hence many structural data. Specific activities, amino-acid compositions, partial sequences and structural homologies of many interferons were determined. Finally, cloned copy DNA (cDNA) fragments derived from specific interferon mRNA, as well as isolated interferon genes, have been sequenced and the data were used to elucidate complete sequences of many interferons with a high degree of confidence.

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The isolation and amino acid/sugar composition of human fibroblastoid interferon.

Cited by 69 publications

References 20 publications

Structure and expression of cloned murine IFN-α genes

Structure and expression of cloned murine IFN-α genes

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

Purification and structural analysis of interferon

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