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https://locus.ufv.br//handle/123456789/18741
Tipo: | Artigo |
Título: | Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
Autor(es): | Guedes, R. N. C. Zhu, K. Y. Kambhampati, S. Dover, B. A. |
Abstract: | Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(β-methyl) thiocholine (AβMTC) and propionylthiocholine (PTC). The efficiency of AChE for hydrolyzing different substrates was ATC > AβMTC > PTC > S-butyrylthiocholine. The enzyme activity was completely inhibited by 10−5 M eserine or BW284C51, but was only partially inhibited by ethopropazine at the same concentration. These results confirmed that the purified enzyme was an typical insect AChE. Non-denaturing and SDS polyacrylamide gel electrophoresis (PAGE) showed only one major molecular form in the purified AChE with a molecular weight of about 107,000 prior to reduction and about 56,000 after reduction, suggesting the homodimer of AChE linked with disulfide bonds. |
Palavras-chave: | Acetylcholinesterase Affinity chromatography Enzyme kinetics Enzyme purification Lesser grain borer Molecular weight Rhyzopertha dominica Substrate specificity |
Editor: | Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology |
Tipo de Acesso: | Elsevier Science Inc. |
URI: | https://doi.org/10.1016/S0742-8413(97)00208-9 http://www.locus.ufv.br/handle/123456789/18741 |
Data do documento: | 30-Out-1997 |
Aparece nas coleções: | Artigos |
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artigo.pdf Until 2100-12-31 | Texto completo | 235,32 kB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
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