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On the Aminoethylation of Proteins

M. A. Raftery 1 and R. David Cole 1

From the 1 From the Department of Biochemistry, University of California, Berkeley, and the Department of Chemistry, California Institute of Technology, Pasadena, California

The reaction of peptide and protein sulfhydryl groups with ethylenimine to give quantitative yields of S-ß-aminoethylcysteinyl residues has been studied. Optimal conditions for tryptic hydrolysis of peptide bonds at the carboxyl terminus of such residues are described for the case of insulin B chain. Separation and identification of peptides obtained in this manner illustrate the applicability of the method to cleavage of polypeptide chains.

Submitted on February 11, 1966


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