Purification of human erythrocyte porphobilinogen deaminase.
Human erythrocyte porphobilinogen deaminase was isolated using ammonium sulphate fractionation and heat treatment, Sephadex G-25 and G-100 chromatography, di-ethylamino-ethyl anion-exchange chromatography, chromatofocusing over a pH gradient of 7-4 and, finally, hydrophobic interaction chromatography on a phenyl-Sepharose column. The enzyme appeared pure as judged by sodium-dodecylsulphate-polyacrylamide gel electrophoresis with silver staining, and yielded a 7 115-fold purification.
Department of Medicine, University of Cape Town.
A V
AV
Corrigall
P N
PN
Meissner
R E
RE
Kirsch
D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D011163:Hydroxymethylbilane Synthase / Q000302:isolation & purification*
D011163:Hydroxymethylbilane Synthase