title: L-dopa decarboxylase in Ceratitis capitata white puparia and human: a comparative study.
abstract: 1. L-DOPA decarboxylase (DDC) from Ceratitis capitata and from human kidney have been purified by the same methodology. 2. Both enzymes show mol. wts of 100,000, consisting of two identical mol. wt subunits and solely decarboxylate L-DOPA. 3. In the presence of 5-hydroxytryptophan (5-HTP) only the DDC activity from human kidney is remarkably reduced. 4. Addition of exogenous coenzyme is essential only for human DDC activity. 5. Polyclonal antibodies, raised against DDC purified from insects or humans, cross-react with both antigens.
authors: Department of Biochemistry, Cell and Molecular Biology and Genetics, University of Athens, Greece.
authors: D G
authors: DG
authors: Mappouras
authors: E G
authors: EG
authors: Fragoulis
mesh_terms: D000818:Animals; D002412:Cations; D004175:Diptera / Q000201:enzymology*; D004296:Dopa Decarboxylase / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008970:Molecular Weight; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D013045:Species Specificity; D013379:Substrate Specificity
chemical_list: D002412:Cations; D011732:Pyridoxal Phosphate; D004296:Dopa Decarboxylase