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1983 (1)
1978 (1)
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1Author    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 
2Author    Jan AhlersRequires cookie*
 Title    Identification of Functional Croups of Pig Kidney Alkaline Phosphatase by Specific Inhibitors  
 Abstract    Inactivation studies with 17 group-specific inhibitors showed that amino, hystidyl and tyrosyl residues probably are components of the active and/or regulatory sites of pig kidney alkaline phosphatase. 
  Reference    (Z. Naturforsch. 30c, 829 [1975]; received July 17/September 19 1975) 
  Published    1975 
  Keywords    Pig Kidney Alkaline Phosphatase, Active Site, Inactivation Studies, Group-Specific Inhibitors 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0829_n.pdf 
 Identifier    ZNC-1975-30c-0829_n 
 Volume    30 
3Author    DhirendraL. NandiRequires cookie*
 Title      
 Abstract    The 14C labelled inactive protein obtained by sodium borohydride reduction of the enzyme, porphobilinogen syn­ thase of R h od op se u d om on a s sp h eroid es, in the presence of [4 -u C ] 5-aminolevulinic acid, gave on acid hydrolysis and subsequent electrophoresis or two-dimensional chromato­ graphy a m ajor radioactive spot which was confirmed to be N -f-[4-(-5am inovaleric acid) ] lysine (A L A -ly s in e) by comparing its co-chromatographic and electrophoretic be ­ haviour with the chemically synthesized A L A -lysin e. A n e -N H , group of lysine residue of porphobilinogen synthase, is thus the binding site of the substrate, 5-aminolevulinic acid. 
  Reference    Z. Naturforsch. 33c, 799 (1978); received A p ril 25/June 6 1978 
  Published    1978 
  Keywords    Borohydride Reduction, L abelled Protein, Hydrolysis Lysine, Active Site 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0799_n.pdf 
 Identifier    ZNC-1978-33c-0799_n 
 Volume    33