Abstract
The reactions of trypsin, trypsinogen, acetyltrypsinogen, and an enzymically active fragment of trypsinogen with N-bromosuccinimide have been explored. Under the conditions used, the reagent selectively oxidized the tryptophan residues without significant cleavage of tryptophyl peptide bonds. The marked difference in reactivity of tryptophan in trypsin and trypsinogen is ascribed to differences in their secondary or tertiary structure. Enzymic inactivation (trypsin) or loss of activatability (trypsinogen) was studied as a function of the oxidative modification of tryptophan. Such partially inactivated enzyme preparations still had their DFP phosphorylation sites intact. At least one tryptophan residue may be needed for activity. This demonstrates that an intact phosphorylation site per se is not sufficient for enzymic activity.
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