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

: Böhm, J.; Otto, B.; Schöne, B.; Slodowski, O.

European Journal of Biochemistry 202 (1991), No.3, pp.1133-1140
ISSN: 0014-2956
Journal Article
Fraunhofer ITA ( ITEM) ()
amino acid sequence; base sequence; cell line; glutamine; interferon-gamma; recombinant interferon-gamma

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.