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...
Guardado en:
| Autores principales: | , , |
|---|---|
| Formato: | JOUR |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p93_WiderdeXifra |
| Aporte de: |
| Sumario: | 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. |
|---|