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Threonine and serine dehydratase activity in the buffalo liver-fluke Fasciola indica
Published online by Cambridge University Press: 05 June 2009
Abstract
Serine dehydratase was found to be five times more active than threonine dehydratase in the liver-fluke Fasciola indica. The latter was not affected by L-isoleucine. Optimum pH for both enzymes was found to be 9.0 in tris-universal buffer. Seven metallic ions tested did not accelerate the enzyme activity, but produced different effects on two enzymes. Two different enzymes probably exist for the two aminoacids, L-threonine and L-serine.
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