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Irreversible inhibition of pancreatic lipase by bis‐ p ‐nitrophenyl methylphosphonate
Author(s) -
Sikk P.,
Osa A.,
Aaviksaar A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80605-0
Subject(s) - tributyrin , lipase , pancreatic lipase , chemistry , residue (chemistry) , enzyme , triacylglycerol lipase , emulsion , chromatography , biochemistry , organic chemistry
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°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.