Tyrosinreiche Proteine im Ameisensäure‐Extrakt von reduzierter Wolle

摘要: An investigation has been made of the acid soluble protein fractions wool that reduced with benzylmercaptane and treated methyliodide. When this modified was shaken in dilute formic (50 v/v) at room temperature for 1 hour, 7% a material dissolved. After dialysis subsequent lyophylisation isolated, shown to be heterogeneous by paper electrophoresis. Fractionation on Sephadex G-75 acetic gave more than six components relatively high content tyrosine phenylalanine. One these fractions, obtained good yield, purified rechromatography. For further separation fraction subjected ion exchange chromatography Dowex (x2) columns. By stepwise elution buffers decreasing pH-values, containing 8 M urea, four subfractions were obtained. The amino compositions wool, extraction, after gel filtration one subfraction are given. In all three an increase glycine, phenylalanine observed low amounts basic acidic acids. The final step characterised endgroup determinations. Dnp-glycine only N-terminal traces Dnp-alanine as contaminant. Hydrazinolysis resulted C-terminus. After digestion trypsin chymotrypsin number peptides different chain lengths obtained, indicating tyrosyl residues had accumulated larger arginyl-peptides present. Sedimentation measurements ultracentrifugation indicated weight average apparent molecular range 9,000 13,000. This is agreement 16,400 derived from amount calculated composition. The analytical results show represents single polypeptide residue about hundred aminoacids which fifty