INACTIVATION OF TRYPSIN AND CHYMOTRYPSIN WITH A PHOTOSENSITIVE PROBE

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Abstract
The photosensitive inactivation of trypsin and chymotrypsin by 4-fluoro-3-nitrophenyl azide (FNPA) is described. A dark inhibition occurred at elevated probe concentrations, and was reversible. The enzymes were stable to photolysis in the absence of probe. Photolytic inactivation of trypsin and chymotrypsin with FNPA was irreversible, and occurred in minutes at concentrations of FNPA where dark inhibition is negligible. The photoprobe was equally effective at pH 3 or pH 8. Nonspecific inactivation appears to be low, as evidenced by stability of glucose oxidase and peroxidase to photolysis with FNPA.