摘要
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.
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.
