Modification of aspartic acid residues to induce trypsin cleavage.
1,2-Diaminoethane and diaminomethane were coupled to aspartic acid residues in small peptides by means of a water-soluble carbodiimide. The resulting modified side chains sufficiently resembled lysine for trypsin to cleave the peptides. Similar modification of glutamic acid residues in peptides gave little or no susceptibility to trypsin.
Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
T T
TT
Wang
N M
NM
Young
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000737:chemistry; D002234:Carbodiimides; D066298:In Vitro Techniques; D007202:Indicators and Reagents; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
D002234:Carbodiimides; D007202:Indicators and Reagents; D010455:Peptides; D001224:Aspartic Acid; D014357:Trypsin