Aminoethylation of SH

This modification is generally performed to introduce new points for tryptic cleavage within the polypeptide chain (Lindley 1956 Raftery 

In principle, reduction and aminoethylation of disulfide-containing proteins, after modification of lysyl and arginyl side chains, should lead to a derivative which can be selectively cleaved by trypsin at S-aminoethylcysteinyl residues. Such a sequence of reactions has been applied to a y-globulin (Slobin and Singer 1968). 

The S-aminoethylcysteine content of the protein derivative can readily be determined following acid hydrolysis of the protein under the usual conditions, and amino acid analysis ( 2.5.4). 

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