The reaction of chymotrypsin and diisopropylphosphorofluoridate II. The structure of two DP-substituted peptides from chymotrypsin-DP
1958; Elsevier BV; Volume: 27; Linguagem: Inglês
10.1016/0006-3002(58)90386-x
ISSN1878-2434
AutoresR.A. Oosterbaan, P. Kunst, J. van Rotterdam, Jules Cohen,
Tópico(s)Advanced Proteomics Techniques and Applications
Resumo1. The amino acid sequence of two diisopropylphosphoryl-substituted peptides obtained from α-chymotrypsin-DP by enzyme hydrolysis was established as: glycyl-aspartyl-seryl-glycyl-glycyl-prolyl-leucine and glycyl-aspartyl-seryl-glycyl-glycyl-proline, respectively. 2. The experimental results strongly suggest that the diisopropylphosphoryl group is attached to the hydroxyl group of the seryl residue. 3. The significance of the investigated peptides in respect to the DFP-binding and ester-splitting ability of α-chymotrypsin is discussed.
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