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Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum

A protein with a molecular weight of 17,400 daltons and an isoelectric point at pH 4.9 has been isolated from the blood serum of healthy donors by successive ion-exchange chromatography of QAE-Sephadex A-50, affinity chromatography on DNA-cellulose, and polyacrylamide gel electrophoresis, in the pre...

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Detalles Bibliográficos
Autores principales: Mavlanov, G. T., Auelbekov, S. A., Aslanov, Kh. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Kluwer Academic Publishers-Plenum Publishers 1986
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088120/
https://www.ncbi.nlm.nih.gov/pubmed/32214421
http://dx.doi.org/10.1007/BF00574738
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author Mavlanov, G. T.
Auelbekov, S. A.
Aslanov, Kh. A.
author_facet Mavlanov, G. T.
Auelbekov, S. A.
Aslanov, Kh. A.
author_sort Mavlanov, G. T.
collection PubMed
description A protein with a molecular weight of 17,400 daltons and an isoelectric point at pH 4.9 has been isolated from the blood serum of healthy donors by successive ion-exchange chromatography of QAE-Sephadex A-50, affinity chromatography on DNA-cellulose, and polyacrylamide gel electrophoresis, in the presence of sodium dodecyl sulfate. The protein isolated, like interferon, suppresses the development of the cytopathogenic action of the viruses of vesicular stomatitis and murine ecephalomyocarditis in cultures of human cells of the L-41 and M-19 lines. The amino acid composition of the protein isolated differs from those of various fractions of human interferons.
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spelling pubmed-70881202020-03-23 Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum Mavlanov, G. T. Auelbekov, S. A. Aslanov, Kh. A. Chem Nat Compd Article A protein with a molecular weight of 17,400 daltons and an isoelectric point at pH 4.9 has been isolated from the blood serum of healthy donors by successive ion-exchange chromatography of QAE-Sephadex A-50, affinity chromatography on DNA-cellulose, and polyacrylamide gel electrophoresis, in the presence of sodium dodecyl sulfate. The protein isolated, like interferon, suppresses the development of the cytopathogenic action of the viruses of vesicular stomatitis and murine ecephalomyocarditis in cultures of human cells of the L-41 and M-19 lines. The amino acid composition of the protein isolated differs from those of various fractions of human interferons. Kluwer Academic Publishers-Plenum Publishers 1986 /pmc/articles/PMC7088120/ /pubmed/32214421 http://dx.doi.org/10.1007/BF00574738 Text en © Plenum Publishing Corporation 1986 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Mavlanov, G. T.
Auelbekov, S. A.
Aslanov, Kh. A.
Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title_full Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title_fullStr Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title_full_unstemmed Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title_short Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
title_sort isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088120/
https://www.ncbi.nlm.nih.gov/pubmed/32214421
http://dx.doi.org/10.1007/BF00574738
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