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

Okamura, H.; Berthold, Wolfgang; Hood, Leroy; Hunkapiller, Michael W.; Inoue, Masafumi; Smith-Johannsen, Heidi; Tan, Y. H.

doi:10.1021/bi00557a028

Cited by 45 publications

(12 citation statements)

References 24 publications

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“…n and t�e sequence of the first 19 amino acids were determmed. ThiS sequence confirmed and extended those reported earlier for the first 13 [43,44], and 10 residues [45]. Subsequently, this se quence was shown to be identical to that predicted from the nucleotide sequence of the cloned DNA.…”

Section: Interferons With Novel Propertiessupporting

confidence: 87%

Purification, Bacterial Expression, and Biological Activities of the Human Interferons

Langer

Pestka

1984

Journal of Investigative Dermatology

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The structural and functional complexity of the hu man interferon system has become increasingly evident. More than eight different alpha (leukocyte) interferons are expressed in induced human cells in culture. Many of these have been purified by a combination of methods, including high-performance liquid chromatography. Moreover, at least 12 different human leukocyte inter ferons have been cloned, and several have been effi ciently expressed in Escherichia coli and other orga nisms. The availability of purified species of leukocyte interferon, both natural and recombinant, has allowed structural work to be done, including amino acid se quence determinations, chemical modification studies, and the crystallization of one species. The purified ma terial has also been used for the production of mono clonal antibodies with various specificities that are proving invaluable in rapid assays and purification techniques. Testing of the purified species for their rel ative potency in antiviral, antiproliferative, and immu nomodulatory assays has begun to demonstrate the func tional uniqueness and diversity of the purified alpha interferons. Hybrid interferon genes have been synthe sized by splicing together parts of various cloned inter feron genes. The resulting hybrid proteins have been valuable in establishing structure/function relation ships. In several cases, the functional properties of the hybrid protein were novel and unpredicted from the properties of the parental molecules.Interferon was discovered by Isaacs and Lindenmann during an investigation of the phenomenon of viral interference, wherein infection by one virus produces resistance to subse quent infection by other, apparently unrelated viruses. Their work [1,2] and that of others [3] demonstrated that cells could respond to challenge with a virus or with other substances (subsequently termed inducers) by producing a substance that could confer upon other cells resistance to subsequent viral attack. This substance, termed interferon, was characterized as a protein that had some species specificity, but that was fairly nonspecific in protecting against a wide range of viruses.Since that time, the complexity of the system has increased as more interferon species within an organism have been rec ognized and characterized and biological effects have beenThe chemical heterogeneity of the interferons has become increasingly evident (Table I). It was found that interferons produced by different cell types were either stable or labile at pH 2. This lead to the designation of types I and II, respectively.Further work demonstrated that there were two main antigen-

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Section: Interferons With Novel Propertiessupporting

confidence: 87%

Purification, Bacterial Expression, and Biological Activities of the Human Interferons

Langer

Pestka

1984

Journal of Investigative Dermatology

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“…The purity of the interferon was verified by NaDodSO4/PAGE. The purified interferon was used as an immunogen to generate antibodies in New Zealand White rabbits as described (17 Habenicht et al. (21).…”

Section: Methodsmentioning

confidence: 99%

Rapid and transient rise in diacylglycerol concentration in Daudi cells exposed to interferon.

Yap¹,

Teo²,

McCoy³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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“…Knight and Fahey, 1981) developed a method for purifying crude fibroblast interferon using two steps of Blue Sepharose chromatography. Tan and colleagues obtained pure fibroblast interferon by a two-step procedure consisting of adsorption/desorption on controlled-pore glass beads and Concanavalin A-Sepharose chromatography (Tan et al, 1979) or by immune affinity chromatography (Okamura et al, 1980), and Heine and Billiau (1981) obtained pure fibroblast interferon by adsorption/desorption on controlled-pore glass beads followed by chromatograpy on zinc chelate agarose. Friesen et al obtained pure fibroblast interferon from serumcontaining medium by affinity chromatography followed by HPLC (Friesen et al, 1981).…”

Section: Early-day Production and Purification Of Natural Human Intermentioning

confidence: 99%

“…Friesen et al obtained pure fibroblast interferon from serumcontaining medium by affinity chromatography followed by HPLC (Friesen et al, 1981). Virtual 100% purity of some of these preparations was validated by N-terminal amino acid sequence determination Okamura et al, 1980).…”

Section: Early-day Production and Purification Of Natural Human Intermentioning

confidence: 99%

Interferons: The pathways of discovery

Billiau

2007

Journal of Clinical Virology

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

Cited by 45 publications

References 24 publications

Purification, Bacterial Expression, and Biological Activities of the Human Interferons

Purification, Bacterial Expression, and Biological Activities of the Human Interferons

Rapid and transient rise in diacylglycerol concentration in Daudi cells exposed to interferon.

Interferons: The pathways of discovery

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