Molecular cloning, expression and characterization of acylpeptide hydrolase in the silkworm, Bombyx mori
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- 作者：Ping Fu ; Wei Sun ; Ze Zhang ; zezhang@cqu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：APH ; Acylpeptide hydrolase ; AChE ; Acetylcholinesterase ; BMs ; Basement membranes ; BSA ; Bovin serum albumin ; DDP IV ; Dipeptidyl peptidase IV ; DTT ; Dithiothreitol ; DAPI ; 4&prime ; 6-diamidino-2-phenylindole ; E. coli ; Escherichia coli ; EDTA ; Ethylenediaminetetraacetic acid ; FITC ; Fluorescein isothiocyanate ; Pi ; Isoelectric point ; IPTG ; Isopropythio-β-D-galactoside ; NJ ; Neighbor-joining ; OP ; Organophosphorus ; PMSF ; Phenylmethylsulphonyl fluoride ; PBS ; Phosphate buffered saline ; PCR ; Polymerase chain
- 刊名：Gene
- 出版年：2016
- 出版时间：10 April 2016
- 年：2016
- 卷：580
- 期：1
- 页码：8-16
- 全文大小：2005 K
文摘
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A putative silkworm Bombyx mori APH gene was cloned and sequenced in insects.
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Heterologous expression of BmAPH gene in E. coli showed that BmAPH has acylpeptide hydrolase activity toward the traditional substrate, Ac–Ala–pNA.
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The enzyme activity of BmAPH was inhibited by the OP compounds in vitro and in vivo, suggesting that it may be involved in OP insecticides resistance of silkworm.
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Immunohistochemistry analysis showed that BmAPH protein was localized in the basement membranes in head and midgut.