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Updated: Aug 13, 2026

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Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
Purification and properties of ornithine racemase from Clostridium sticklandii
1Department of Biochemistry, China Medical College, Taichung 404, Taiwan. hpchen@mail.cmc.edu
Journal of Bacteriology
|March 14, 2000
Abstract:
Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an M(r) of 92, 000, with a K(m) for L-ornithine of 0.77 +/- 0.05 mM and a k(cat) of 980 +/- 20 s(-1).
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