title: Uroporphyrinogen decarboxylases from human erythrocytes: purification, complete separation and partial characterization of two isoenzymes.
abstract: 1. Two distinct molecular forms of uroporphyrinogen decarboxylase have been completely separated and highly purified from human erythrocytes. 2. Each protein, with molecular masses of about 52-54 kDa and 35 kDa, are apparently composed of a single polypeptide chain. 3. They may form a functional decarboxylating complex for heme biosynthesis.
authors.affiliation: Department of Internal Medicine, School of Medicine, University of California, Davis, Sacramento 95817.
authors.forename: S K
authors.initials: SK
authors.lastname: Mukerji
authors.forename: N R
authors.initials: NR
authors.lastname: Pimstone
mesh_terms: D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014575:Uroporphyrinogen Decarboxylase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D014575:Uroporphyrinogen Decarboxylase