Molecular and enzymatic characterization of acid phosphatase from venom of Scleroderma guani
作者： Nai-Yong Liu , Xiao-Hong Fan , Zhi-Quan Zhang , Guo-Xing Wu , Jia-Ying Zhu
DOI: 10.1016/J.ASPEN.2017.10.012
关键词: Enzyme assay 、 Open reading frame 、 Enzyme 、 Amino acid 、 Biochemistry 、 Biology 、 Gene expression 、 Venom 、 Acid phosphatase 、 Molecular biology 、 Gene
摘要: Abstract Acid phosphatase (ACPase) is a common component in venom of parasitoids. Although extensive researches regarding this enzyme have been conducted many other organisms, its characteristics as venomous are still sparsely known. In study, we aimed to reveal the gene expression patterns, and structural biochemical properties an ACPase from Scleroderma guani. The cloned open reading frame S. guani was 1218 bp encoding 406 deduced amino acids, shared 40% 41% identities ACPases venoms Apis mellifera Pteromalus puparum, respectively. analysis implied functions differences honeybee ACPase. qPCR showed that abundantly expressed apparatus, most highly adult stage after one three days emergence. Activity assay using p-nitrophenyl phosphate substrate revealed optimal pH temperature for 4.8 45 °C, NaF effective inhibitor it. results will enrich our knowledge toxin, which may contribute further uncovering role involved parasitism.
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