Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: dissection of the stabilizing effects of coenzyme binding and subunit interaction.

Pyruvate oxidase from Lactobacillus plantarum is a homotetrameric flavoprotein with strong binding sites for FAD, TPP, and a divalent cation. Treatment with acid ammonium sulfate in the presence of 1.5 M KBr leads to the release of the cofactors, yielding the stable apoenzyme. In the present study,...

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Hlavní autoři: Risse, B., Stempfer, G., Rudolph, R., Möllering, H., Jaenicke, R.
Médium: Artigo
Jazyk:Inglês
Vydáno: Cold Spring Harbor Laboratory Press 1992
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142136/
https://ncbi.nlm.nih.gov/pubmed/1304899
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