Purification and characterisation of L-DOPA decarboxylase from pharate pupae of Ceratitis capitata.  A comparison with the enzyme purified from the white prepupae. 
In this paper we describe the purification of L-DOPA decarboxylase (DDC) to homogeneity from the developmental stage just before the eclosion (pharate pupae) of Ceratitis capitata.  The enzyme was found to have a mol wt of approximately 100,000 and to be composed of two identical subunits (50,000 mol wt each).  Polyclonal antibodies raised against the isolated enzyme reacted with the 50,000 dalton subunit and precipitated enzyme activity.  Furthermore, properties of the enzyme isolated from the pharate pupa stage, were compared with those of DDC purified from the white prepupa stage with respect to substrate specificity, response to polyclonal antibodies, behaviour towards different cations and dependence of enzyme activity on the concentration of pyridoxal phosphate.