Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/3474
Title: Inhibition studies on calf pregastric esterase: The enzyme has no functional thiol group
Authors: Timmermans, MYJ
Reekmans, G
TEUCHY, Henri 
KUPERS, Luc 
Issue Date: 1996
Publisher: PORTLAND PRESS
Source: BIOCHEMICAL JOURNAL, 314. p. 931-936
Abstract: 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 partial inhibition with dodecyldithio-5-(2-nitrobenzoic acid) was observed, but the same degree of inhibition was caused by the non-esterified fatty acid C-12:0. PGE shows a great sequence similarity to gastric lipases. Gastric lipases have three cysteine residues, and two of these form a disulphide bridge. Blocking the remaining free cysteine with thiol reagents inactivates the gastric lipases. The fact that PGE is not inhibited by thiol reagents indicates that PGE has no functional free thiol group. The PGE cDNA codes only for two cysteines, and their involvement in the formation of a disulphide bridge was demonstrated.
Notes: NV JOS THEYS,B-3500 HASSELT,BELGIUM.Timmermans, MYJ, LIMBURGS UNIV CENTRUM,DEPT BIOCHEM,UNIV CAMPUS,B-3590 DIEPENBEEK,BELGIUM.
Document URI: http://hdl.handle.net/1942/3474
Link to publication: http://www.biochemj.org/bj/314/bj3140931.htm
ISI #: A1996UC24500032
Type: Journal Contribution
Appears in Collections:Non-affiliated authors

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