A 15-kD interferon-induced protein and its 17-kD precursor: expression in Escherichia coli, purification, and characterization. 1989

N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
Central Research and Development Department, E.I. du Pont de Nemours and Company, Inc., Wilmington, DE 19880-0328.

Using recombinant DNA technology, a 15-kD interferon (IFN)-induced protein and its 17-kD precursor have been expressed in Escherichia coli to obtain sufficient quantities of each protein for the investigation of their biological roles. Both the 15-kD and 17-kD proteins have been purified to homogeneity and crystallized. The recombinant 15-kD protein has an identical reversed-phase HPLC elution profile to that of the native 15-kD protein purified from human cells. Furthermore, the recombinant 15-kD and 17-kD proteins have identical amino- and carboxy-terminal amino acid sequences to those predicted from the DNA sequence. The native and recombinant 15-kD proteins give identical tryptic peptide maps, and the recombinant 17-kD protein gives only one additional tryptic peptide. We conclude that the recombinant 17-kD and 15-kD proteins are identical to the 17-kD precursor and the 15-kD stable product synthesized in human cells in response to IFN stimulation. In addition, we have demonstrated that the recombinant 17-kD precursor protein can be converted to the 15-kD protein by cytoplasmic extracts of human cells.

UI MeSH Term Description Entries
D007372 Interferons Proteins secreted by vertebrate cells in response to a wide variety of inducers. They confer resistance against many different viruses, inhibit proliferation of normal and malignant cells, impede multiplication of intracellular parasites, enhance macrophage and granulocyte phagocytosis, augment natural killer cell activity, and show several other immunomodulatory functions. Interferon
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011498 Protein Precursors Precursors, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial

Related Publications

N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
August 1993, The Journal of biological chemistry,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
July 1987, Biochimica et biophysica acta,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
February 1990, The Journal of biological chemistry,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
April 1988, The Journal of biological chemistry,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
March 1993, FEBS letters,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
February 1996, The Journal of laboratory and clinical medicine,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
January 1981, Reviews of infectious diseases,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
June 2011, Protein and peptide letters,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
February 2013, The Journal of biological chemistry,
N Feltham, and M Hillman, and B Cordova, and D Fahey, and B Larsen, and D Blomstrom, and E Knight
August 2009, Molecular and cellular biochemistry,
Copied contents to your clipboard!