Abstract:
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.
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Citas:
---------- APA ----------
Wider de Xifra, E.A., Stella, A.M. & Del C. Batlle, A.M.
(1978)
. Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells. Plant Science Letters, 11(2), 93-98.
http://dx.doi.org/10.1016/0304-4211(78)90111-6---------- CHICAGO ----------
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"
. Plant Science Letters 11, no. 2
(1978) : 93-98.
http://dx.doi.org/10.1016/0304-4211(78)90111-6---------- MLA ----------
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"
. Plant Science Letters, vol. 11, no. 2, 1978, pp. 93-98.
http://dx.doi.org/10.1016/0304-4211(78)90111-6---------- VANCOUVER ----------
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. 1978;11(2):93-98.
http://dx.doi.org/10.1016/0304-4211(78)90111-6