Uroporphyrinogen decarboxylases from human erythrocytes: purification, complete separation and partial characterization of two isoenzymes.
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.
Mukerji
S K
SK
Department of Internal Medicine, School of Medicine, University of California, Davis, Sacramento 95817.
Pimstone
N R
NR
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*
D007527:Isoenzymes; D014575:Uroporphyrinogen Decarboxylase