Purification and characterization of recombinant murine immune interferon

• Published in: FEBS letters Vol. 205; no. 2; pp. 200 - 204
• Main Authors: Nagata, Kiyoshi, Kikuchi, Norihisa, Ohara, Osamu, Teraoka, Hiroshi, Yoshida, Nobuo, Kawade, Yoshimi
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 15.09.1986; Elsevier
• Subjects: Amino Acid Sequence; Analysis of the immune response. Humoral and cellular immunity; Animals; Applied sciences; Biological and medical sciences; Escherichia coli; Escherichia coli - analysis; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Genetic Vectors; HPLC, high-performance liquid chromatography; Immunobiology; interferon; Interferon-gamma - isolation & purification; Interferon-gamma - metabolism; Lymphokines, interleukins ( function, expression); Mice; Other techniques and industries; Peptide Fragments - isolation & purification; peptide mapping; Recombinant murine immune interferon Purification Terminal analysis Peptide mapping; Recombinant murine immune interferonPurificationTerminal analysisPeptide mapping; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Regulatory factors and their cellular receptors; rMu-IFN-γ, recombinant murine immune interferon; SDS-PAGE, polyacrylamide gel electrophoresis; HPLC, high-performance liquid chromatography; SDS-PAGE, polyacrylamide gel electrophoresis; rMu-IFN-γ, recombinant murine immune interferon; Recombinant murine immune interferon Purification Terminal analysis Peptide mapping; Peptide map; Vertebrata; Mammalia; Purification; Mouse; Rodentia; Genetic engineering; Lymphokine; Aminoacid sequence; Gamma interferon
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(86)80897-3

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.