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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1978
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paper:paper_03044211_v11_n2_p93_WiderdeXifra2023-06-08T15:29:59Z Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells Wider de Xifra, Eva Adela Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen 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. 1978 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044211_v11_n2_p93_WiderdeXifra http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p93_WiderdeXifra |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
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. |
author |
Wider de Xifra, Eva Adela Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen |
spellingShingle |
Wider de Xifra, Eva Adela Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen Porphyrin biosynthesis-immobilized enzymes and ligands. IX. Studies on δ-aminolaevulinate synthetase from cultured soybean cells |
author_facet |
Wider de Xifra, Eva Adela Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen |
author_sort |
Wider de Xifra, Eva Adela |
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 |
publishDate |
1978 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044211_v11_n2_p93_WiderdeXifra http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p93_WiderdeXifra |
work_keys_str_mv |
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1768545691513126912 |