Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. T...
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todo:paper_03008177_v16_n2-3_p97_Stella2023-10-03T15:17:45Z Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose Stella, A.M. de Xifra, E.W. Batlle, A.M.d.C. enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. The coupling yield was rather high. The insolubilized enzyme requires both anaerobiosis and a thiol activator for maximal activity. It can be stored at 4 °C for long periods with little loss of activity and it can be repeatedly used without alteration of its enzymic capacity. Attachment of ALA-D to the gel has led to an enhanced thermal stability. pH optima of free and bound enzyme was the same while a small decrease in the Km of the matrix bonded ALA-D as compared to that of the soluble enzyme was observed. The use of the fixed-ALA-D for the preparation of PBG is described. © 1977 Dr. W. Junk b.v. Publishers. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p97_Stella |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature |
| spellingShingle |
enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature Stella, A.M. de Xifra, E.W. Batlle, A.M.d.C. Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| topic_facet |
enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature |
| description |
Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. The coupling yield was rather high. The insolubilized enzyme requires both anaerobiosis and a thiol activator for maximal activity. It can be stored at 4 °C for long periods with little loss of activity and it can be repeatedly used without alteration of its enzymic capacity. Attachment of ALA-D to the gel has led to an enhanced thermal stability. pH optima of free and bound enzyme was the same while a small decrease in the Km of the matrix bonded ALA-D as compared to that of the soluble enzyme was observed. The use of the fixed-ALA-D for the preparation of PBG is described. © 1977 Dr. W. Junk b.v. Publishers. |
| format |
JOUR |
| author |
Stella, A.M. de Xifra, E.W. Batlle, A.M.d.C. |
| author_facet |
Stella, A.M. de Xifra, E.W. Batlle, A.M.d.C. |
| author_sort |
Stella, A.M. |
| title |
Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| title_short |
Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| title_full |
Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| title_fullStr |
Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| title_full_unstemmed |
Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose |
| title_sort |
porphyrin biosynthesis. immobilized enzymes iv. studies on aminolaevulate dehydratase attached to sepharose |
| url |
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p97_Stella |
| work_keys_str_mv |
AT stellaam porphyrinbiosynthesisimmobilizedenzymesivstudiesonaminolaevulatedehydrataseattachedtosepharose AT dexifraew porphyrinbiosynthesisimmobilizedenzymesivstudiesonaminolaevulatedehydrataseattachedtosepharose AT batlleamdc porphyrinbiosynthesisimmobilizedenzymesivstudiesonaminolaevulatedehydrataseattachedtosepharose |
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1807317495931994112 |