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		题名	作者	年代	出处	被引量
	1	Isolation, purification and characterization of a new organphosphorus hydrolase OPHC2显示文摘A bacterium with the capability of degrading organphosphorus, identified as Pseudomonas pseudoaicaligenes, is isolated from OP-treated soil. The organphosphorus hydrolase OPHC2 from this bacterium has been purified and characterized. OPHC2 has optimum activity for the reaction at 65℃ and pH 9.0 with methyl parathion as a substrate, it also shows good thermal and pH stability. Most metal ions and chemicals have no effect on the activity of OPHC2. The analyses of nucleotide sequence encoding OPHC2 and amino acid sequence of OPHC2 show that there are lower homologies with those of organphosphorus hydrolase reported in GenBank.	WUNingfeng DENGMinjie SHIXiuyun LIANGGuoyi YAOBin FANYunliu	2004	Chinese Science Bulletin2004，49，3：	6
	2	Cloning and expression of ophc2,a new organphosphorus hydrolase gene显示文摘The amino acid sequences of N-terminal and internal peptide of OPHC2,purified from Pseudomonas pseudoalcaligenes strain C2-1 in our lab,are determined.The full-length organphosphorus hydrolase gene ophc2 is cloned by PCR using the degenerate primers designed according to the sequences and future inverse PCR.The ophc2 gene is 975 bp long with G+C content of 63%,comprising one open reading frame encoding a polypeptide of 324 amino acids with a molecular weight of 36 kD.The nucleotide sequence of ophc2 shows low homolo- gies with those organphosphorus hydrolase genes deposited in Gen- Bank,one of which exhibits the highest homology of 46.4% with ophc2.The organphosphorus hydrolase protein expressed in E.coli bears normal bioactivity.	WUNingfeng DENGMinjie LIANGGuoyi CHUXiaoyu YAOBin FANYunliu	2004	Chinese Science Bulletin2004，49，12：	3

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