Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
Heterogeneity of proteinase inhibitors in the water-soluble organic matrix from the oyster nacre
Bédouet, L.; Duplat, D.; Marie, A.; Dubost, L.; Berland, S.; Rousseau, M.; Milet, C.; Lopez, E. (2007). Heterogeneity of proteinase inhibitors in the water-soluble organic matrix from the oyster nacre. Mar. Biotechnol. 9(4): 437-449. https://dx.doi.org/10.1007/s10126-007-7120-y
In: Marine Biotechnology. Springer-Verlag: New York. ISSN 1436-2228; e-ISSN 1436-2236
|  |
| Trefwoorden |
Inhibitors > Metabolic inhibitors > Enzyme inhibitors > Proteinase inhibitors
Nacre
Marien/Kust |
| Author keywords |
cathepsins; nacre; papain; Pinctada; proteinase inhibitors; proteinase K |
| Auteurs | | Top |
- Bédouet, L.
- Duplat, D.
- Marie, A.
- Dubost, L.
|
- Berland, S.
- Rousseau, M.
- Milet, C.
- Lopez, E.
|
|
| Abstract |
We extracted proteinase inhibitors from the nacre of the oyster Pinctada margaritifera with water. Mixing the nacre powder with water for 20 h led to a water-soluble fraction [0.24% (wt/wt) of nacre]. After dialysis of the water-soluble matrix through 6- to 8-kDa and 0.5-kDa membranes, the proteinase inhibitors were divided into low and high molecular weight fractions that contained inhibitors of papain, bovine cathepsin B, and human cathepsin L. We studied the heterogeneity of the inhibitors after separating the low molecular weight fraction according to charge and hydrophobicity. After multistep purification, mass spectrometry analysis revealed that a potent inhibitory fraction contained several molecules. This observation demonstrates the difficulties encountered in attempting to isolate individual metabolites from the complex mixture of molecules present in nacre matrix. Interestingly, the low molecular weight fraction contained specific inhibitors that could discern between cathepsin B and cathepsin L. The nacre organic inhibitors were active against several cysteine proteinases, yet they were more specific in relation to serine proteinases, because only proteinase K was inhibited. These results demonstrate, for the first time, the presence of active proteinase inhibitors in the mollusc shell, and it is possible that these inhibitors may play a role in either protection of proteins involved in shell formation or in defense against parasites, or both. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
