Προβολή άρθρου

A procedure for the purification of l-DOPA decarboxylase (DDC) from the white puparia of Ceratitis capitata is described. Polyacrylamide gel electrophoresis (PAGE) in the presence or absence of sodium dodecyl sulfate (SDS) revealed the homogencity of the final preparation. The enzyme molecular weight determined by gel filtration was about 100,000 dalton. A single band appeared on SDS-PAGE of a molecular weight estimated at about 48,000. Therefore a dimeric structure is proposed for the DDC molecule from C. capitata. The enzyme exhibits a remarkable specificity only towards l-DOPA and none of the ions tested present either a strong inhibitory or stimulatory effect on enzyme activity.