Affordable Access

Inactivation of human pancreatic lipase by 5-dodecyldithio-2-nitrobenzoic acid.

Authors
  • Gargouri, Y
  • Cudrey, C
  • Mejdoub, H
  • Verger, R
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
Mar 15, 1992
Volume
204
Issue
3
Pages
1063–1067
Identifiers
PMID: 1551387
Source
Medline
License
Unknown

Abstract

Both thiol groups of native human pancreatic lipase can react with the new hydrophobic sulfhydryl reagent 5-dodecyldithio-2-nitrobenzoic acid (Dod-S-NbS) in the absence of a denaturing agent. Here we describe for the first time the covalent and stoichiometric modification of the inaccessible SHII group of native pancreatic lipase, using a 16-fold molar excess of this hydrophobic sulfhydryl reagent. A direct correlation was found to exist between the covalent modification of this SHII group and the loss of lipase activity. The question has not yet been answered, however, as to how Dod-S-NbS reaches the SHII-containing residue, whereas classical hydrophilic sulfhydryl reagents are unable to do so. This difference in reactivity may be attributable to the hydrophobic character of Dod-S-NbS and its potential capacity to form aggregates inducing a conformational change in the lipase molecule.

Report this publication

Statistics

Seen <100 times