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

• Autores: Bustos, N.; Stella, A.M.; Xifra, E.A.W.D.; C. Batlle, A.M.D.
• Año de publicación: 1980
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: Int. J. Biochem. 1980;12(5-6):745-749
• Materia: butanol; chloroform; porphobilinogen synthase; blood and hemopoietic system; enzyme purification; erythrocyte; human cell; in vitro study; normal human; preliminary communication; Enzymes, Immobilized; Erythrocytes; Human; Porphobilinogen Synthase; Support, Non-U.S. Gov't; Thiosulfate Sulfurtransferase
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

1. 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 and affinity chromatography yielding a 1600-fold purified enzyme, is described. 2. 2. By oxidation of Sephadex G-25 with NaIO4, a polyaldehyde, is obtained which can be covalently bound to the ALA-D; however the immobilized enzyme is inactive, because essential ε{lunate}-amino groups at the active site were involved in the coupling. Similar experiments with another enzyme, Rhodanese, resulted in an active insolubilized preparation. 3. 3. By suspending the carrier-enzyme in buffer, slow solubilization with simultaneous release of protein occurs, indicating that this approach might find important therapeutical applications in the treatment of enzyme deficiencies. © 1980.
Fil:Bustos, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:C. Batlle, A.M.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.