Title: Purification and Partial cDNA Sequence of Acetylcholinesterase from a Korean Strain of the Housefly, Musca domestica Im DJ, Kim WT, Boo KS Ref: Journal of Asia-Pacific Entomology, 7:81, 2004 : PubMed
Acetylcholinesterase (AChE) was purified from adult heads of a Korean housefly, Musca domestica, strain (KNIH) by affinity chromatography on trimethyl (ffj-aminophenyl) ammonium chloride resin. The purified AChE showed the purification factor over 400-fold and the specific activity of about 290 umol/min/mg. The housefly has both the membrane-bound and the soluble forms of AChE. Only the membrane-bound form of the housefly AChE was isolated by Triton X-114 phase partition and revealed on the native gel. The maximum activities of the purified AChE were shown at pH 7.5-8.5 and 40-45degC. Partial cDNA of AChE (795bp) of the KNIH strain showed that its deduced amino acid sequence shared high similarity with that of insecticide-resistant type of insect AChE.
        
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Im DJ, Kim WT, Boo KS (2004) Purification and Partial cDNA Sequence of Acetylcholinesterase from a Korean Strain of the Housefly, Musca domestica Journal of Asia-Pacific Entomology7: 81-87
Im DJ, Kim WT, Boo KS (2004) Journal of Asia-Pacific Entomology7: 81-87