Specificity of trypsin. Cleavage of aspartic acid 101 derivatives of lysozyme by trypsin.
The beta-carboxyl group of Asp 101 was modified with several amine nucleophiles by the amine-carbodiimide procedure and the trypsin susceptibilities of the derivatives were analyzed by peptide mapping. The (aminoethyl)asparaginyl peptide bond was completely cleaved by trypsin but the (3-aminopropyl)asparaginyl bond was not. When the positive charge was in the proper position, large residues such as (2-[imidazol-4(5)-ylmethylamino]ethyl) asparagine or (11-amino-3,-6,9-triazaundecyl)asparagine were susceptible to trypsin.
D000588:Amines; D000596:Amino Acids / Q000032:analysis; D001224:Aspartic Acid; D002851:Chromatography, High Pressure Liquid; D009113:Muramidase; D010446:Peptide Fragments / Q000032:analysis*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
D000588:Amines; D000596:Amino Acids; D010446:Peptide Fragments; D001224:Aspartic Acid; D009113:Muramidase; D014357:Trypsin