Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications

摘要: Abstract 1. A method for purifying human erythrocytes ALA-D, using a mixture of n -butanol and chloroform, which denature hemoglobin, followed by ammonium sulphate fractionation affinity chromatography yielding 1600-fold purified enzyme, is described. 2. By oxidation Sephadex G-25 with NaIO 4 , polyaldehyde, obtained can be covalently bound to the ALA-D; however immobilized enzyme inactive, because essential ϵ-amino groups at active site were involved in coupling. Similar experiments another Rhodanese, resulted an insolubilized preparation. 3. suspending carrier-enzyme buffer, slow solubilization simultaneous release protein occurs, indicating that this approach might find important therapeutical applications treatment deficiencies.