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. 1977 Aug 1;165(2):375–383. doi: 10.1042/bj1650375

The structure of L-lactate oxidase from Mycobacterium smegmatis.

P A Sullivan, C Y Soon, W J Schreurs, J F Cutfield, M G Shepherd
PMCID: PMC1164910  PMID: 921754

Abstract

1. An improved purification was developed for L-lactate oxidase from Mycobacterium smegmatis. 2. The mol.wt. of the native enzyme by a sedimentation-equilibrium analysis was 345 000, and other ultracentrifuge methods gave values in the range 345 000-350 000. 3. An amino acid analysis, determinations of protein and flavin, a sedimentation-velocity analysis and an approach to equilibrium analysis gave values for the subunit mol.wt. in the range 43 500-47 000. 4. It was concluded that L-lactate oxidase contains eight subunits of mol.wt. 43 500. 5. Cross-linking of the subunits with dimethyl suberimidate and electron-microscopy studies were consistent with an octameric structure.

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Selected References

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