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...

Full description

Saved in:
Bibliographic Details
Published inChemistry of natural compounds Vol. 22; no. 2; pp. 195 - 200
Main Authors Mavlanov, G T, Auelbekov, S A, Aslanov, Kh A
Format Journal Article
LanguageEnglish
Published United States Kluwer Academic Publishers-Plenum Publishers 01.01.1986
Subjects
Acid Composition
Dodecyl
Interferon
Polyacrylamide
Sodium Dodecyl
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0009-3130
1573-8388
DOI:10.1007/BF00574738