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

doi:10.1111/j.1432-1033.1991.tb16481.x

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Article

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

European journal of biochemistry - 18 Dec 1991

Slodowski O, Böhm J, Schöne B, Otto B

Abstract excerpt

The biological function of the 20 C-terminal amino acids of human interferon-gamma (IFN-gamma) was examined by recombinant DNA methodology. Six truncated IFN-gamma analogues were produced by modification of the 3' end of the coding sequence of the cloned gene, insertion into a vector with the trc promoter and expression of the recombinant IFN-gamma analogue genes in Escherichia coli strain JM 105. The IFN-gamma...

Topics

Amino Acid Sequence
Base Sequence
Cell Line
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Encephalomyocarditis virus
Genetic Variation
Glutamine
Humans
Interferon-gamma
Leucine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Microbial Sensitivity Tests

Molecular Sequence Data

Mutagenesis, Site-Directed

Oligodeoxyribonucleotides

Protein Conformation

Protein Denaturation

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 1662603
DOI: 10.1111/j.1432-1033.1991.tb16481.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1662603-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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