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.