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  4. Carboxy-terminal truncated rhuIFN-gamma with a substitution of Gln133 or Ser132 to leucine leads to higher biological activity than in the wild type
 
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1991
Journal Article
Title

Carboxy-terminal truncated rhuIFN-gamma with a substitution of Gln133 or Ser132 to leucine leads to higher biological activity than in the wild type

Abstract
The biological function of the 20 C-terminal amino acids of human Interferon-gamma (IFN-gamma) was examined. Six truncated IFN-gamma analogues were produced by recombinant DNA technique and expressed in Escherichia coli. In four of these constructions the C-terminal amino acid is replaced by leucine. The antiviral activities of the variants lacking 14 or more amino acids are less than 2 per cent of the control. The variant C-10 Leu exhibits a fourfold higher antiviral activity compared to complete IFN-gamma. CD analysis reveals no significant differences for the variants, but C-10 Leu shows a higher temperature stability.
Author(s)
Böhm, J.
Otto, B.
Schöne, B.
Slodowski, O.
Journal
European Journal of Biochemistry  
Language
English
ITA  
Keyword(s)
  • amino acid sequence

  • base sequence

  • cell line

  • glutamine

  • interferon-gamma

  • recombinant interferon-gamma

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