| Title : The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution - Montenegro_2008_Chem.Biol.Interact_175_336 |
| Author(s) : Montenegro MF , Moral-Naranjo MT , Paez de la Cadena M , Campoy FJ , Munoz-Delgado E , Vidal CJ |
| Ref : Chemico-Biological Interactions , 175 :336 , 2008 |
| Abstract : Butyrylcholinesterase (BuChE) and acetylcholinesterase (AChE) display both esterase and aryl acylamidase (AAA) activities. Their AAA activity can be measured using o-nitroacetanilide (ONA). In human samples depleted of acetylcholinesterase, we noticed that the ratio of amidase to esterase activities varied depending on the source, despite both activities being due to BuChE. Searching for an explanation, we compared the activities of BuChE molecular forms in samples of human colon, kidney and serum, and observed that BuChE monomers (G(1)) hydrolyzed o-nitroacetanilide much faster than tetramers (G(4)). This fact suggested that association might cause differences in the AAA site between single and polymerized subunits. This and other post-translational modifications in BuChE subunits probably determine their level of AAA activity. The higher amidase activity of monomers could justify the presence of single BuChE subunits in cells as a way to preserve the AAA activity of BuChE, which could be lost by oligomerization. |
| ESTHER : Montenegro_2008_Chem.Biol.Interact_175_336 |
| PubMedSearch : Montenegro_2008_Chem.Biol.Interact_175_336 |
| PubMedID: 18452906 |
Montenegro MF, Moral-Naranjo MT, Paez de la Cadena M, Campoy FJ, Munoz-Delgado E, Vidal CJ (2008)
The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution
Chemico-Biological Interactions
175 :336
Montenegro MF, Moral-Naranjo MT, Paez de la Cadena M, Campoy FJ, Munoz-Delgado E, Vidal CJ (2008)
Chemico-Biological Interactions
175 :336