Threonine and serine dehydratase activity in the buffalo liver-flukeFasciola indica

Abstract

AbstractSerine dehydratase was found to be five times more active than threonine dehydratase in the liver-flukeFasciola 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.