Appearance: White to pale yellowish white powder
Purity: ≥98.0% (HPLC)
MW: C10H20INOS, 329.24
Storage Condition: 0-5°C
Shipping Condition: Ambient temperature
Keyword: Acetylcholinesterase, AChE activity, Alzheimer
Acetylcholinestrase (AChE) is one of the important enzymes to control signal transduction of nervous system by decomposing acetylcholine (neurotransmitter). It is found at brain and blood. Since the activity of the enzyme is reduced by organic phosphate, insecticides and pesticides containing carbamate, it is used as indicator of exposure in these chemicals. In addition, AChE inhibitors have been attracting attention as a therapeutic drug for Alzheimer's disease, because contents of acetylcholine is reduced by neuropathy in Alzheimer’s disease1).
Ellman method is widely used for AChE activity measurement2), 3). However, the selectivity of acetylcholine is poor against AChE, because acetylcholine reacts with Butylcholinestrase (BChE) in vivo. Since BChE inhibitors are required to determine accurate AChE activity, the experimental procedure is complicated4)-6).
MATP+ is a novel AChE substrate that have been developed by the national Institute of Radiological Sciences (Fig 1 and Fig 2)7). Because MATP+ performs much higher selectivity toward AChE, it allows to measure easily and selectively AChE activity without the addition of BChE inhibitor. The reagent is useful for AChE activity measurement in whole blood and AChE nervous tissue staining using Karovsky-Roots method.
Fig 1. The principle of AChE activity mesurement with MATP+
Fig 2. The selectivity of AChE with MATP+ (Ellman method)
1) H. Sugimoto, FOLIA PHARMACOL JPN, 2004, 124, 163.
2) V. Battissi, M. R. C. Schetinger, L. D. K. Maders, K. F. Santos, M. D. agatini, M. C. Correa, R. M. Spanevello, M. do C. Araujo and V. M. Morsch, Clin. Chim. Acta, 2009, 402, 114.
3) M. S. Garcia-Ayllon, M. X. Silveyra, A. Candela, A. Compan, J. Claria, R. Jover, M. Perez-Mateo, V. Felipo, S. Martinez, J. Galceran and J. Saez-Valero, Hepatology, 2006, 43(3), 444.
4) S. Brimijoin and P. Hammond, J. Neurochemistry, 1988, 51(4), 1227.
5) F. Worek, U. Mast, D. Kiderlen, C. Diepold and P. Eyer, Clin. Chim. Acta, 1999, 288, 73.
6) R. S. Naik, B. P. Doctor and A. Saxena, Chem. Biol. Interact., 2008, 175, 298.
7) T. Kikuchi, T. Okamura, K. Fukushi and T. Irie, Biol. Pharm. Bull., 2010, 33(4), 702.