Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
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...
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todo:paper_0020711X_v12_n5-6_p745_Bustos2023-10-03T14:17:41Z Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications Bustos, N. Stella, A.M. Xifra, E.A.W.D. C. Batlle, A.M.D. 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Bustos, N. Stella, A.M. Xifra, E.A.W.D. C. Batlle, A.M.D. Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Bustos, N. Stella, A.M. Xifra, E.A.W.D. C. Batlle, A.M.D. |
| author_facet |
Bustos, N. Stella, A.M. Xifra, E.A.W.D. C. Batlle, A.M.D. |
| author_sort |
Bustos, N. |
| title |
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| title_short |
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| title_full |
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| title_fullStr |
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| title_full_unstemmed |
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications |
| title_sort |
studies on erythrocyte aminolaevulinate dehydratase i. its purification and possible therapeutic applications |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos |
| work_keys_str_mv |
AT bustosn studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications AT stellaam studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications AT xifraeawd studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications AT cbatlleamd studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications |
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1807322037532753920 |