Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells
Soybean callus δ-aminolaevulinate synthetase (ALA-S) has been covalently attached to Sepharose 4B. The optimal conditions for binding have been determined. The water-insoluble ALA-S retained 40% of the activity of the original soluble preparation, the coupling yield was also high. Sepharose - ALA-S...
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todo:paper_03044211_v11_n2_p93_WiderdeXifra2023-10-03T15:20:53Z Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells Wider de Xifra, E.A. Stella, A.M. Del C. Batlle, A.M. Soybean callus δ-aminolaevulinate synthetase (ALA-S) has been covalently attached to Sepharose 4B. The optimal conditions for binding have been determined. The water-insoluble ALA-S retained 40% of the activity of the original soluble preparation, the coupling yield was also high. Sepharose - ALA-S could be stored at 4°C for periods up to 40 days with only 25% loss of activity and it could be repeatedly used with little alteration of its enzymic activity. pH optima of the free and bound enzyme were the same. © 1978. Fil:Wider de Xifra, E.A. 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:Del C. Batlle, A.M. 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_03044211_v11_n2_p93_WiderdeXifra |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| description |
Soybean callus δ-aminolaevulinate synthetase (ALA-S) has been covalently attached to Sepharose 4B. The optimal conditions for binding have been determined. The water-insoluble ALA-S retained 40% of the activity of the original soluble preparation, the coupling yield was also high. Sepharose - ALA-S could be stored at 4°C for periods up to 40 days with only 25% loss of activity and it could be repeatedly used with little alteration of its enzymic activity. pH optima of the free and bound enzyme were the same. © 1978. |
| format |
JOUR |
| author |
Wider de Xifra, E.A. Stella, A.M. Del C. Batlle, A.M. |
| spellingShingle |
Wider de Xifra, E.A. Stella, A.M. Del C. Batlle, A.M. Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| author_facet |
Wider de Xifra, E.A. Stella, A.M. Del C. Batlle, A.M. |
| author_sort |
Wider de Xifra, E.A. |
| title |
Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| title_short |
Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| title_full |
Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| title_fullStr |
Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| title_full_unstemmed |
Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| title_sort |
porphyrin biosynthesis-immobilized enzymes and ligands. ix. studies on δ-aminolaevulinate synthetase from cultured soybean cells |
| url |
http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p93_WiderdeXifra |
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