| Abstract: | The reaction of porcine pancreatic lipase with an organophosphorus compound bis-p-nitrophenyl methylphosphonate (BNMP) resulted in the complete and irreversible inhibition of lipase activity on tributyrin emulsion (25 degrees C, pH 7.5, 40 mM Na-veronal-HCl buffer) whereas the activity of the enzyme on p-nitrophenyl acetate solution remained unchanged. The BNMP-modified enzyme did not bind on hydrophobic interfaces (siliconized glass beads). Tyr 49 was presumed to be the modification site, and the conclusion has been made that this residue is implicated in the interface recognition site of pancreatic lipase. |
