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Purification and characterization of 3,4-dihydroxyphenylalanine decarboxyase from pig kidney.

A procedure for 3,4-dihydroxyphenylalanine decarboxylase from pig kkdney purification is described in detail. The preparation has no detectable impurity on electrophoresis and on ultracentrifugation and authors. However two significant differences are observed: a different stimulation of activity by added pyridoxal 5'-phosphate and a nearly complete decarboxylation of L-3,4-dihydroxyphenylalanine in absence of added coenzyme. Absorption, fluorescence and circular dichroism properties of the coenzyme-apoenzyme interaction are also described. The results are consistent with the existence of at least four coenzyme-apoenzyme complexes, three of them active.