Identification of One of the L-Serine Dehydratase Isoenzymes from Rat Liver as L-Homoserine Dehydratase.

摘要

The higher molecular weight L-serine dehydratase was purified from rat liver and fractionated into two active components by Sephadex G-200 gel chromatography. On the basis of molecular weight, ultracentrifugal pattern and substrate specificity of the major component, it was concluded that this component is identical to L-homoserine dehydratase. Some misinterpretations which have been derived from the work on L-serine dehydratase in animal tissues are pointed out. (Author)