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. 1983 Feb;153(2):658–664. doi: 10.1128/jb.153.2.658-664.1983

Purification and properties of Selenomonas ruminantium lysine decarboxylase.

Y Kamio, Y Terawaki
PMCID: PMC221682  PMID: 6401702

Abstract

Selenomonas ruminantium, a strictly anaerobic, gram-negative bacterium isolated from sheep rumen, contains lysine decarboxylase (Y. Kamio et al., J. Bacteriol. 145:122-128, 1981). This report describes the synthesis, purification, and characterization of the enzyme. Lysine decarboxylase was synthesized in cells grown in chemically defined medium without lysine. The enzyme was purified approximately 1,800-fold to electrophoretic homogeneity. The native enzyme of approximate molecular weight 88,000 consisted of two identical subunits, each with a molecular weight of 44,000. Several properties of the enzyme were determined and compared with those of the lysine decarboxylases from Escherichia coli and Bacterium cadaverisis.

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Selected References

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