Importance of sulfhydryl group for rabbit gastric lipase activity
- 29 August 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 236 (2) , 383-387
- https://doi.org/10.1016/0014-5793(88)80061-9
Abstract
We have shown recently that rabbit gastric lipase (RGL) purified from gastric tissue presents catalytic properties comparable with those of human gastric lipase (HGL). We report here that only one sulfhydryl group was modified per molecule of native RGL after incubation at pH 8.0 with 5,5′-dithiobis(2-nitrobenzoic acid) (NbS2) for 4 h or 4,4′-dithiopyridine (4-PDS) for 60 min. With both reagents, a direct correlation was found between the modification of one sulfhydryl group per enzyme molecule and loss of RGL activity. Incubation of RGL with the new hydrophobic sulfhydryl reagent, dodecyldithio-5-(2-nitrobenzoic acid) (C12-NbS), at 30-fold molar excess, at pH 3.0, 5.0 and 8.0, induced immediate and complete inactivation of RGL. Unlike NbS2 and 4-PDS, C12-NbS almost instantaneously stopped the course of tributyrin hydrolysis by RGL, in contrast to porcine pancreatic lipase (PPL). RGL can be included with HGL in the group of sulfhydryl enzymes.Keywords
This publication has 7 references indexed in Scilit:
- Kinetic assay of human gastric lipase on short- and long-chain triacylglycerol emulsionsGastroenterology, 1986
- Purification and properties of an acid lipase from human gastric juiceBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982
- On the sulfhydryl groups of porcine pancreatic lipase and their possible role in the activity of the enzymeBiochimica et Biophysica Acta (BBA) - Enzymology, 1971
- The sulfhydryl groups of pancreatic lipaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridineArchives of Biochemistry and Biophysics, 1967
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951