On the active site of horse-liver ali esterase I. Reaction of the enzyme with diisopropylphosphorofluoridate
article
Horse-liver ali esterase reacts with DFP to form the enzymically inactive DP-enzyme. With isonitrosoacetone diisopropylphosphate is released from the inhibited enzyme; this is accompanied by a recovery of the enzymic activity. In order to investigate the chemical nature of the DFP-binding site of ali esterase the DP-enzyme was digested with pepsin. Essentially one DP-peptide was formed which contained per mole of DP-group the following moles of amino acid residues: alanine (1), glutamic acid or glutamine (2), glycine (3), and serine (2). © 1959.
TNO Identifier
226698
ISSN
00063002
Source
BBA - Biochimica et Biophysica Acta, 33(2), pp. 387-395.
Pages
387-395
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