Inhibition studies on calf pregastric esterase: the enzyme has no functional thiol group.

@article{Timmermans1996InhibitionSO,
  title={Inhibition studies on calf pregastric esterase: the enzyme has no functional thiol group.},
  author={M Y Timmermans and Gunter Reekmans and Henri Teuchy and L. J. P. Kupers},
  journal={The Biochemical journal},
  year={1996},
  volume={314 ( Pt 3)},
  pages={
          931-6
        }
}
Pregastric esterase (PGE) (EC 3.1.1.3) was purified to homogeneity from calf pharyngeal tissue. The enzyme had an apparent molecular mass of 50 kDa, as determined by SDS/PAGE. The serine-binding reagent diethyl p-nitrophenyl phosphate was a potent inhibitor of PGE. This is in accordance with the claim that a functional serine residue is necessary for the lipolytic activity of lipases. PGE was not inhibited by the thiol reagents 5,5'-dithiobis(2-nitrobenzoic acid) or 4,4'-dithiopyridine. A… CONTINUE READING