[Specific cleavage of the cysteine-peptide bond of thermitase].
Cyanylation and N-cysteine peptide bond cleavage of thermitase using 2-nitro-5-thiocyanobenzoic acid results in the formation of two peptide fragments (mol. wt. 20 000 and 10 000) in high yield (about 90%). These peptides are well separated by gel filtration on Sephadex G-75 in the preparative scale.
D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D003545:Cysteine / Q000032:analysis*; D003619:Dansyl Compounds / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D010450:Endopeptidases / Q000032:analysis*; D006868:Hydrolysis; D008970:Molecular Weight; D009579:Nitrobenzoates; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013438:Sulfhydryl Compounds / Q000032:analysis
D000596:Amino Acids; D003619:Dansyl Compounds; D009579:Nitrobenzoates; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; C011136:thionitrobenzoic acid; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase; D003545:Cysteine
Spezifische Spaltung der Zystein-Peptidbindung der Thermitase.