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Purification and characterization of recombinant murine immune interferon
Author(s) -
Nagata Kiyoshi,
Kikuchi Norihisa,
Ohara Osamu,
Teraoka Hiroshi,
Yoshida Nobuo,
Kawade Yoshimi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80897-3
Subject(s) - recombinant dna , complementary dna , escherichia coli , microbiology and biotechnology , amino acid , biology , peptide sequence , peptide , polyacrylamide gel electrophoresis , gel electrophoresis , interferon , biochemistry , chemistry , gene , enzyme , virology
The recombinant murine immune interferon (rMu‐IFN‐γ) was purified to homogeneity from Escherichia coli harboring the expression vector of murine IFN‐γ. The purified rMu‐IFN‐γ showed an M r of 15000 in SDS‐polyacrylamide gel electrophoresis. Results of amino acid analysis, amino‐ and carboxyl‐terminal analyses and peptide mapping of rMu‐IFN‐γ suggest that it has the complete protein sequence predicted on the basis of cDNA except for lack of four amino acid residues from the mature carboxyl‐terminus.