Darvesh_2001_Cell.Mol.Neurobiol_21_285

Reference

Title : Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin - Darvesh_2001_Cell.Mol.Neurobiol_21_285
Author(s) : Darvesh S , Kumar R , Roberts S , Walsh R , Martin E
Ref : Cellular Molecular Neurobiology , 21 :285 , 2001
Abstract :

1. Acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BuChE, EC 3.1.1.8) are enzymes that catalyze the hydrolysis of esters of choline. 2. Both AChE and BuChE have been shown to copurify with peptidases. 3. BuChE has also been shown to copurify with other proteins such as transferrin, with which it forms a stable complex. In addition, BuChE is found in association with beta-amyloid protein in Alzheimer brain tissues. 4. Since BuChE copurifies with peptidases, we hypothesized that BuChE interacts with these enzymes and that this association had an influence on their catalytic activities. One of the peptidases that copurifies with cholinesterases has specificity similar to trypsin, hence, this enzyme was used as a model to test this hypothesis. 5. Purified BuChE causes a concentration-dependent enhancement of the catalytic activity of trypsin while trypsin does not influence the catalytic activity of BuChE. 6. We suggest that, in addition to its esterase activity, BuChE may assume a regulatory role by interacting with other proteins.

PubMedSearch : Darvesh_2001_Cell.Mol.Neurobiol_21_285
PubMedID: 11569538

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Citations formats

Darvesh S, Kumar R, Roberts S, Walsh R, Martin E (2001)
Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin
Cellular Molecular Neurobiology 21 :285

Darvesh S, Kumar R, Roberts S, Walsh R, Martin E (2001)
Cellular Molecular Neurobiology 21 :285