Partial purification and characterization of human gamma (immune) interferon.

Yip, Y. K.; Pang, Roy H. L.; Urban, Carl; Vilček, Ján

doi:10.1073/pnas.78.3.1601

Cited by 132 publications

(60 citation statements)

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“…(The same concentration of 6 X 106 mononuclear cells per ml was employed in both types of cultures.) Although the kinetics of IFN production proved to be somewhat variable in the experiments shown in Table 1 In an earlier study we demonstrated that IFN produced in cultures of mononuclear cells derived from platelet residues stimulated with' TPA and PHA had the characteristics of'IFN-'y (14). To ascertain the suitability of the TPA/PHA stimulation for the extraction of IFN-y mRNA we performed the following experiment.…”

Section: Resultsmentioning

confidence: 99%

“…The molecular weight ofhuman IFN-y was recently estimated to be 58,000 ± 3000 by gel filtration (14). The difference between the value based on mRNA size and the apparent size of the IFN-y molecule itselfcould be due to carbohydrate.…”

Section: Discussionmentioning

confidence: 99%

“…IFN activity was assayed by inhibition ofthe cytopathic effect of vesicular stomatitis virus or encephalomyocarditis virus in human GM-258 cells as described (14). Because no reference standard for human IFN-y is available, all results were expressed in "laboratory units" (14).…”

Section: Methodsmentioning

confidence: 99%

“…The latter IFN is usually produced in cultures of lymphocytes exposed to various mitogenic stimuli-e.g., specific antigens or lectins. Recently we described an efficient method of production and partial purification ofhuman IFN-y (14). In this paper we report on the preparation ofbiologically active human IFN-'y mRNA.…”

mentioning

confidence: 99%

“…Production and Extraction of IFN-y mRNA. Induction of IFN-y in human lymphocytes by PHA in the presence of TPA was carried out as described (14). Briefly, mononuclear cells were isolated from lymphocyte-rich "platelet residues" (obtained through the courtesy of Alan Waldman from the New York Blood Center) by centrifugation at 400 X g for 30 min on a Ficoll/Hypaque gradient.…”

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confidence: 99%

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Partial characterization of gamma (immune) interferon mRNA extracted from human lymphocytes.

Taniguchi¹,

Pang²,

Yip³

et al. 1981

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

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Y (immune) interferon (IFN-'y) was induced in cultures of fresh human lymphocytes by combined treatment with a phorbol ester (12-0-tetradecanoylphorbol 13-acetate, TPA) and the T cell mitogen phytohemagglutinin (PHA). Compared to the IFN-y yields obtained with PHA induction alone, the inclusion of TPA caused a significant enhancement of IFN-y production.Poly(A)-containing mRNA was isolated from mononuclear cells induced with TPA and PHA. Injected into Xenopus laevis oocytes, this mRNA preparation gave rise to IFN activity with characteristic properties of human IFN-y. Sucrose density gradient centrifugation analysis showed that IFN-y mRNA sedimented at 15 S, suggesting that it contains a total of about 1400 nucleotides.As a result ofrecent progress in the study ofvarious interferons (IFNs), all known IFNs can be grouped into three major classes designated IFN-a ("leukocyte"), 3 ("fibroblast"), and IFN-'y ("immune"). Identification of the three major IFN classes is based primarily on antigenic differences (1). Additional distinguishing properties include differences in various physicochemical and biological characteristics (2).Several earlier studies showed that mRNA for IFN-a and IFN-f3 can be extracted from cells actively producing IFN. Such IFN mRNA preparations can direct synthesis of biologically active IFN molecules with corresponding specificity when introduced into heterologous animal cells (3), suitable cell-free systems (4-6), or Xenopus laevis oocytes (6-8). Identification of human IFN-a and IFN-,B mRNAs on the basis of their ability to direct the synthesis of homologous, biologically active IFN molecules on injection in X. laevis oocytes made possible the preparation of cDNAs and their cloning in bacteria (9, 10). Comparison of the first available IFN-a and IFN-/3 cDNA sequences indicated only 29% homology between the two IFNs at the amino acid level (11). Recent analysis of human chromosomal gene bank DNA revealed the existence ofat least eight related but distinct IFN-a sequences, differing from each other in about 10-30% of their predicted amino acid residues (12). In contrast, only one subclass ofIFN-,BmRNA has been tentatively identified in addition to the IFN-,f cDNA clone originally isolated (13).Studies of isolated IFN-a and IFN-fB DNA clones and of the corresponding IFN polypeptides produced in bacteria have already provided a wealth ofinformation about the structure and biological properties ofthese IFNs. In addition, cloning ofthese IFN genes in Escherichia coli promises to facilitate the production of large quantities of biologically active IFN.In contrast, much less information is available about IFN-y. The latter IFN is usually produced in cultures of lymphocytes exposed to various mitogenic stimuli-e.g., specific antigens or lectins. Recently we described an efficient method of production and partial purification ofhuman . In this paper we report on the preparation ofbiologically active human IFN-'y mRNA. It is hoped that the preparation of IFN-y mRNA will allow the synthesis ...

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Partial characterization of gamma (immune) interferon mRNA extracted from human lymphocytes.

Taniguchi¹,

Pang²,

Yip³

et al. 1981

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

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Progress toward therapeutic application of interferons, 1979–1983

Borden¹

1984

Cancer

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Interferons differ chemically and biologically from other modalities of cancer treatment. They are proteins that inhibit viral replication, influence subcellular processes, slow cellular proliferation, affect cell differentiation, and modulate immune responses. These regulatory effects on cell function undoubtedly underlie the effects of interferons in malignant disease. As a result of efforts by academia, industry, governments, and organizations such as the American Cancer Society, significant progress has been made over the past 5 years in elucidating structure, improving production, and defining clinical applications of interferons for both virus and malignant disease.

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Protein Production inPseudomonas fluorescens

Chew¹,

Ramseier²,

Retallack³

et al. 2008

Protein Science Encyclopedia

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Originally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4 The sections in this article are Introduction Biology of Pseudomonas fluorescens History and Taxonomy of Pseudomonas fluorescens Strain Biovar I MB101 Cultivation Genomics and Functional Genomics of P. fluorescens Strain MB101 Core Expression Platform for Heterologous Proteins Antibiotic‐free Plasmids using pyrF and proC Gene Deletion Strategy and Re‐usable Markers Periplasmic Secretion and Use of Transposomes Alternative Expression Systems: Anthranilate and Benzoate‐inducible Promoters Production of Heterologous Proteins in P. fluorescens Pharmaceutical Proteins Industrial Enzymes Agricultural Proteins Conclusions Appendix

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Partial purification and characterization of human gamma (immune) interferon.

Cited by 132 publications

References 18 publications

Partial characterization of gamma (immune) interferon mRNA extracted from human lymphocytes.

Partial characterization of gamma (immune) interferon mRNA extracted from human lymphocytes.

Progress toward therapeutic application of interferons, 1979–1983

Protein Production inPseudomonas fluorescens

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