Site-specific mutagenesis of the human fibroblast interferon gene.
- 1 September 1984
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 81 (18), 5662-5666
- https://doi.org/10.1073/pnas.81.18.5662
Abstract
Human fibroblast interferon has three cysteine residues, located at amino acid positions 17, 31, and 141. Using the technique of site-specific mutagenesis with a synthetic oligonucleotide primer, we changed the codon for cysteine-17 to a codon for serine. The resulting interferon, IFN-beta Ser-17, retains the antiviral, natural killer cell activation, and antiproliferative activities of native fibroblast interferon. The purified IFN-beta Ser-17 protein has an antiviral specific activity of 2 X 10(8) units/mg, similar to that of purified native fibroblast interferon. In addition, the purified protein is stable to long-term storage at -70 degrees C.This publication has 18 references indexed in Scilit:
- Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP bindingNature, 1982
- Construction of a functional human suppressor tRNA gene: an approach to gene therapy for β-thalassaemiaNature, 1982
- Purification and molecular characterization of human fibroblast interferonArchives of Biochemistry and Biophysics, 1981
- Properties of a Human Alpha-Interferon Purified fromE. ColiExtractsJournal of Interferon Research, 1981
- Expression of human fibroblast interferon gene in Escherichia coliNature, 1980
- The nucleotide sequence of human fibroblast interferon cDNAGene, 1980
- Site-specific mutagenesis using synthetic oligodeoxyribonucleotide primers: II. In vitro selection of mutant DNAGene, 1979
- Site-specific mutagenesis using synthetic oligodeoxyribonucleotide primers: I. Optimum conditions and minimum oligodeoxyribonucleotide lengthGene, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- DNA Restriction Enzyme from E. coliNature, 1968