title: Biologic activity in a fragment of recombinant human interferon alpha.
abstract: To attempt to locate functionally important regions of the interferon (IFN) molecule, recombinant human IFN-alpha 2 was subjected to proteolytic digestion. The bacterial proteinase thermolysin produced two major complementary fragments, HuIFN-alpha 2-(1-110) and HuIFN-alpha 2-(111-153). After reduction with 2-mercaptoethanol and separation of the two major fragments on NaDodSO4/polyacrylamide gel electrophoresis, antiviral activity persisted in the larger, Mr 12,000, fragment consisting of the amino-terminal 110 amino acids.
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002460:Cell Line; D003001:Cloning, Molecular; D004274:DNA, Recombinant; D005347:Fibroblasts; D006801:Humans; D007370:Interferon Type I / Q000235:genetics* / Q000302:isolation & purification* / Q000633:toxicity; D016898:Interferon-alpha; D007372:Interferons / Q000378:metabolism; D007668:Kidney; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification* / Q000633:toxicity; D011956:Receptors, Cell Surface / Q000378:metabolism; D017471:Receptors, Interferon; D011994:Recombinant Proteins; D012867:Skin; D013820:Thermolysin; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects
chemical_list: D004274:DNA, Recombinant; D007370:Interferon Type I; D016898:Interferon-alpha; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D017471:Receptors, Interferon; D011994:Recombinant Proteins; C040773:interferon, alpha 2(1-110); C040774:interferon, alpha 2(111-153); D007372:Interferons; D013820:Thermolysin