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Modification of aspartic acid residues to induce trypsin cleavage
1Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
Analytical Biochemistry
|December 1, 1978
Abstract:
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.