Inactivation of human pancreatic lipase by 5-dodecyldithio-2-nitrobenzoic acid
| Autor: | C. Cudrey, Hafedh Mejdoub, Youssef Gargouri, Robert Verger |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Conformational change
Protein Conformation Triacylglycerol lipase Biochemistry chemistry.chemical_compound Structure-Activity Relationship Sulfhydryl reagent Humans Sulfhydryl Compounds Lipase Enzyme Inhibitors Pancreas chemistry.chemical_classification Binding Sites biology Sulfhydryl Reagents food and beverages Chemical modification chemistry Nitrobenzoic acid Reagent Nitrobenzoates Thiol biology.protein |
| Zdroj: | European journal of biochemistry. 204(3) |
| ISSN: | 0014-2956 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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