Abstract
The lignostilbenedioxygenase isozyme I and III genes, lsdA and lsdB, were coexpressed within the same Escherichia coli cells. The lignostilbenedioxygenase isozymes produced were separated on QAE anion-exchange column chromatography. Three parts of active fractions corresponding to αα, αβ, and ββ dimers were detected. The purified isozyme from second active fractions corresponded to the native heterogeneous isozyme II.
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Kamoda, S., Terada, T., & Saburi, Y. (2005). Production of heterogeneous dimer lignostilbenedioxygenase II from lsdA and lsdB in Escherichia coli cells. Bioscience, Biotechnology and Biochemistry, 69(3), 635–637. https://doi.org/10.1271/bbb.69.635
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