[Expression of pyruvate oxidase gene sopox from Streptococcus sanguis in E. coli].
OBJECTIVE
To reconstruct the expression plasmid of Sopox gene for further understanding the regulation of its expression.


METHODS
Sopox was recombined with expression vector pBV220 and the expression of Sopox in E. coli JM105 was observed after transformation.


RESULTS
pBV220/Sopox/JM105 expressed a protein with molecular weight of 65 kd on SDS-PAGE after induction, and the expression reached the maximal amount with induction at 42 degrees C for 4 hours.


CONCLUSIONS
Sopox was successfully cloned into pBV220 and expressed in E. coli JM105.
Department of Periodontology, School of Stomatology, WCUMS, Chengdu 610041, China.
B
B
Hou
J
J
Zhang
R
R
Zhang
Y
Y
Zhang
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D018014:Gene Transfer Techniques; D005798:Genes, Bacterial; D010957:Plasmids / Q000235:genetics; D011771:Pyruvate Oxidase / Q000235:genetics*; D013298:Streptococcus sanguis / Q000201:enzymology / Q000235:genetics*
D011771:Pyruvate Oxidase