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[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. CONCLUSION: Sopox was successfully cloned into pBV220 and expressed in E. coli JM105.

Cloning, Molecular↗

[Association, in the same subject, of deletion of the short arm of chromosome 4 (4p-) and of complete deficiency of parahydroxyphenyl-pyruvate oxidase activity in the liver (tyrosinosis)].

The authors report the association in a child of monosomy 4p- and tyrosinosis. They discuss the localization of the para-hydroxyphenylpyruvate oxidase locus on the short arm of chromosome 4. They suggest the study of para-hydroxyphenylpyruvate oxidase activity in each child with monosomy 4p-.

4-Hydroxyphenylpyruvate Dioxygenase↗

Correlation of oxygen utilization and hydrogen peroxide accumulation with oxygen induced enzymes in Lactobacillus plantarum cultures.

Two strains of Lactobacillus plantarum accumulated H2O2 when grown aerobically in a complex glucose based medium. The H2O2 accumulation did not occur immediately on exposure of the culture to O2 but was delayed for a time which, in the case of one strain, was dependent on the amount of inoculum used to seed the culture. The accumulation was always preceded by an increase in the rate of O2 utilization by the cultures. The latter coincided approximately with an increase in specific activity of NADH oxidase, pyruvate oxidase and NADH peroxidase. H2O2 was not a product of NADH oxidase in vitro but was formed in substantial quantities from O2 during oxidation of pyruvate. The three enzymes were induced by O2 and H2O2; the induction of NADH oxidase responded to lower levels of O2 (but not of H2O2) than the pyruvate oxidase or the NADH peroxidase.

Hydrogen Peroxide↗