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1. Sorption, desorption and mobility characteristics of a novel fungicide pyrazoxystrobin in three agricultural soils | |||
Liu Xunyue,Ding Xingcheng | |||
Agronomy 20 January 2012 | |||
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Abstract:Pyrazoxystrobin, (E)-methyl 2-(3-((3-(4-chlorophenyl)-1-methyl- 1H -pyrazol-5-yloxy) methyl) phenyl) -3 - methoxyacrylate, is a novel fungicide developed in China. The adsorption, desorption and mobility characteristics of pyrazoxystrobin on three agricultural soils were studied by using 14C labeled compound. The adsorption of pyrazoxystrobin in soils was correlated to soil organic matter content and soil pH and the sorption has been observed in the order of S2>S1>>S3. Desorption was reflect some of the interactions involved between the pesticides and the soil components, soil pH seems to more influence to pyrazoxystrobin desorption and only about 2.54 to 6.41% of adsorbed pyrazoxystrobin was released. The mobility result, minimum of 95.02% compound residued in the upper 4.0 cm layer, demonstrated the use of pyrazoxystrobin as a fungicide is likely to be safe to groundwater. | |||
TO cite this article:Liu Xunyue,Ding Xingcheng. Sorption, desorption and mobility characteristics of a novel fungicide pyrazoxystrobin in three agricultural soils[OL].[20 January 2012] http://en.paper.edu.cn/en_releasepaper/content/4463029 |
2. Prophenoloxidase-1 (PPO1) cDNA clone and its expression in Diamondback moth Plutella xylostella | |||
Xue Chaobin,Luo Wanchun | |||
Agronomy 10 December 2010 | |||
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Abstract:Phenoloxidase (PO) is a key enzyme in insect development, responsible for catalyzing the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones. In this paper, the prophenoloxidase-1 (PxPPO1) cDNA of Plutella xylostella was cloned by means of reverse transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE). The full-length cDNA consisted of 2838bp, containing an open reading frame (ORF) of 2049bp which encoding 682 amino acids. The molecular mass of the deduced amino acids and the active enzyme was predicted to be 78.56kDa and 72.65 kDa, respectively. The calculated pI was 6.43. BLASTp search and neighbor-joining analysis showed that the deduced amino acid sequence had a high identity to the published sequence of PPO1 from other lepidopterous insects, ranging from 70.5% to 74.6%. Protein signature analysis revealed three conserved regions, including the two copper binding sites characteristic of arthropod PPOs. Semi-quantitative RT-PCR and Real-time PCR indicated that the highest amount of PxPPO1 transcripts in eggs or the 4th instar larvae, followed by the 2nd, the 3rd instar larvae, prepupae and pupa. | |||
TO cite this article:Xue Chaobin,Luo Wanchun. Prophenoloxidase-1 (PPO1) cDNA clone and its expression in Diamondback moth Plutella xylostella[OL].[10 December 2010] http://en.paper.edu.cn/en_releasepaper/content/4396723 |
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