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Purification of human erythrocyte porphobilinogen deaminase
A V Corrigall1, P N Meissner, R E Kirsch
1Department of Medicine, University of Cape Town.
Abstract:
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.
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