کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1982765 | 1062314 | 2009 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae
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کلمات کلیدی
5,5-dithio-bis(2-nitrobenzoic acid)propionylthiocholine iodideBW284C51butyrylthiocholine iodideNi-NTABTCATCDTNBPTCAChE - آهیAcetylthiocholine iodide - اتیل تیوکولین یدیدOrganophosphate - ارگانوفسفاتAcetylcholinesterase - استیل کولین استرازsodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدOrganophosphorous compounds - ترکیبات ارگاسم فسفرCholinergic synapse - سیناپس کولینرژیکMalaria - مالاریاInsecticide resistance - مقاومت به حشره کشnickel-nitrilotriacetic acid - نیکل نیتریلوتوریکات اسیدMosquito - پشهCarbamate - کارباماتhigh performance liquid chromatography - کروماتوگرافی مایع با کارایی بالاHPLC - کروماتوگرافی مایعی کارا
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش حشره شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae](/preview/png/1982765.png)
چکیده انگلیسی
Acetylcholinesterases (AChEs) and their genes from susceptible and resistant insects have been extensively studied to understand the molecular basis of target site insensitivity. Due to the existence of other resistance mechanisms, however, it can be problematic to correlate directly a mutation with the resistant phenotype. An alternative approach involves recombinant expression and characterization of highly purified wild-type and mutant AChEs, which serves as a reliable platform for studying structure-function relationships. We expressed the catalytic domain of Anopheles gambiae AChE1 (r-AgAChE1) using the baculovirus system and purified it 2,500-fold from the conditioned medium to near homogeneity. While KM's of r-AgAChE1 were comparable for ATC, AβMTC, PTC, and BTC, Vmax's were substantially different. The IC50's for eserine, carbaryl, paraoxon, BW284C51, malaoxon, and ethopropazine were 8.3, 72.5, 83.6, 199, 328, and 6.59 Ã 104 nM, respectively. We determined kinetic constants for inhibition of r-AgAChE1 by four of these compounds. The enzyme bound eserine or paraoxon stronger than carbaryl or malaoxon. Because the covalent modification of r-AgAChE1 by eserine occurred faster than that by the other compounds, eserine is more potent than paraoxon, carbaryl, and malaoxon. Furthermore, we found that choline inhibited r-AgAChE1, a phenomenon related to the enzyme activity decrease at high concentrations of acetylcholine.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Insect Biochemistry and Molecular Biology - Volume 39, Issue 9, September 2009, Pages 646-653
Journal: Insect Biochemistry and Molecular Biology - Volume 39, Issue 9, September 2009, Pages 646-653
نویسندگان
Haobo Jiang, Siwei Liu, Picheng Zhao, Carey Pope,