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1992 (1)
1987 (1)
1983 (1)
1Author    Klaus Leonhardt, Timm Anke, Elisabeth Hillen-Maske, Wolfgang SteglichRequires cookie*
 Title    6-Methylpurine, 6-Methyl-9-ß-D-ribofuranosylpurine, and 6-Hydroxymethyl-9-ß-D-ribofuranosylpurine as Antiviral Metabolites of Collybia maculata (Basidiomycetes) [1]  
 Abstract    6 -M eth y lp u rin e (1), 6-m eth yl-9-ß -D -rib ofu ran osylp u rin e (2) and 6 -h yd roxym eth yl-9-ß -D -rib o-fu ra n o sy lp u rin e (3) w ere isolated from m ycelial cu ltures o f Collybia maculata and their an tifu n gal, c y to to x ic and antiviral activities in v estig a ted . T h is is the first rep ort on th e natural o ccu rren ce o f th e se c o m p o u n d s. 
  Reference    Z. Naturforsch. 42c, 420 (1987); received November 5 1986 
  Published    1987 
  Keywords    Collybia maculata, Basidiomycetes, Nucleosides, 6-Methylpurine, Antiviral Activity 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0420.pdf 
 Identifier    ZNC-1987-42c-0420 
 Volume    42 
2Author    Anders Ljungqvist, Karl Folkers+Requires cookie*
 Title    Synthesis of a Combined Fragment of Interferon, AeHuIFN a A(30-43)-(123-137)-NH2 Interferon May not be a Sychnologieal Peptide * AeHuIFN a A( 30-43)-( 123-137)-NH2, Ac-Leu-Lys-Asp-Arg-His-Asp-Phe-Gly-Phe- Pro-Gln-Glu-Glu-Phe-Phe-Gln-Arg-Ile-Thr-Leu-Tyr-Leu-Lys-Glu-Lys-Lys-Tyr-Ser- Pro-NH2 was  
 Abstract    synthesized toward encompassing the "active site" of the interferons. The design of this 29-amino acid peptide was based on considerations of homology between the different interferons and on combining two regions of interferons, and on known and predicted structural features. The peptide was characterized by amino acid analysis, thin layer chromatography in several systems, and by HPLC. As tested, the peptide neither showed antiviral activity nor blocked antiviral activity of interferon, indicating that the active site was not encompassed or that interferon may not be a sychnologieal peptide. 
  Reference    Z. Naturforsch. 38b, 1249—1252 (1983); received June 24 1983 
  Published    1983 
  Keywords    Interferon, Peptide Synthesis, Antiviral Activity, Synthetic Fragment, Active Site 
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 TEI-XML for    default:Reihe_B/38/ZNB-1983-38b-1249.pdf 
 Identifier    ZNB-1983-38b-1249 
 Volume    38 
3Author    M. Ax Schönfelder, Ute Janott, Roland Frötschl, Karl-W Olfgang, M. Undry, G. Ünter, AdamRequires cookie*
 Title    Purification of Antiviral Proteins with Ribosome-Inactivating Properties from Plants  
 Abstract    A generally applicable highly effective purification method for antiviral plant proteins, selective for those with ribosome-inactivating properties, was developed. It involved affinity chromatography on Cibacron Blue Sepharose of the extracted plant sap after acid-ethanol precipitation and finally cation exchange chromatography on Mono S (Pharmacia). After the second chromatography step electrophoretically pure proteins from the four plant species, Chenopodium amaranticolor, Dianthus barbatus, Phytolacca americana and Spinacia oleracea, were obtained. These proteins inhibited infection of test plants with alfalfa mosaic virus and in vitro translation of TMV-RNA. The apparent molecular weights of the purified proteins were determined by SDS polyacrylamide gel electrophoresis as: 29 kDa for C. amaranticolor, 33 kDa for D. barbatus, 29 kDa for P. americana and 36 kDa for S. oleracea. Comparisons of the proteins by indirect ELISA and by Western blotting with polyclonal antisera from rabbits revealed that all four proteins were serologically related but not identical. In addition all four proteins were found to be glycosylated. 
  Reference    Z. Naturforsch. 47c, 731—738 (1992); received June 9/August 19 1992 
  Published    1992 
  Keywords    Antiviral Activity, Ribosome-Inactivating Proteins, Isolation, Serological Comparison, Glycosylation 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0731.pdf 
 Identifier    ZNC-1992-47c-0731 
 Volume    47