Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells
Soybean callus succinyl CoA synthetase (succinate : CoA ligase, (ADP-forming), EC 6.2.1.5), has been chemically bound to Sepharose 4B and some of its properties have been studied. The optimal conditions for binding have been determined. The immobilized enzyme retained 48% of the activity of the solu...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00052744_v523_n1_p245_WiderdeXifra |
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todo:paper_00052744_v523_n1_p245_WiderdeXifra2023-10-03T14:03:29Z Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells Wider de Xifra, E.A. Batlle, A.M.D.C. enzyme porphyrin succinyl coenzyme a synthetase animal experiment higher plant in vitro study Cells, Cultured Coenzyme A Ligases Drug Stability Enzymes, Immobilized Kinetics Plants Porphyrins Soybeans Succinate-CoA Ligases Soybean callus succinyl CoA synthetase (succinate : CoA ligase, (ADP-forming), EC 6.2.1.5), has been chemically bound to Sepharose 4B and some of its properties have been studied. The optimal conditions for binding have been determined. The immobilized enzyme retained 48% of the activity of the soluble enzyme and the coupling yield amounted to 50%. Sepharose · succinyl CoA synthetase can be stored at 4°C for periods up to 90 days with only 25% loss of activity; it can also be repeatedly used without alteration of its enzymic activity. The complex showed enhanced thermal stability; pH optimum was between 7.0 and 8.0 for the bound enzyme, and 8.0 for the free enzyme. A general decrease in the Michaelis-Menten constants for the different substrates of the insoluble enzyme, as compared with values obtained for the free enzyme, was found. Plots of the rate product formation against ATP concentration changed from sigmoideal for the soluble succinyl CoA synthetase to hyperbolic for the immobilized enzyme. © 1978. Fil:Wider de Xifra, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.D.C. 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_00052744_v523_n1_p245_WiderdeXifra |
| 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 porphyrin succinyl coenzyme a synthetase animal experiment higher plant in vitro study Cells, Cultured Coenzyme A Ligases Drug Stability Enzymes, Immobilized Kinetics Plants Porphyrins Soybeans Succinate-CoA Ligases |
| spellingShingle |
enzyme porphyrin succinyl coenzyme a synthetase animal experiment higher plant in vitro study Cells, Cultured Coenzyme A Ligases Drug Stability Enzymes, Immobilized Kinetics Plants Porphyrins Soybeans Succinate-CoA Ligases Wider de Xifra, E.A. Batlle, A.M.D.C. Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| topic_facet |
enzyme porphyrin succinyl coenzyme a synthetase animal experiment higher plant in vitro study Cells, Cultured Coenzyme A Ligases Drug Stability Enzymes, Immobilized Kinetics Plants Porphyrins Soybeans Succinate-CoA Ligases |
| description |
Soybean callus succinyl CoA synthetase (succinate : CoA ligase, (ADP-forming), EC 6.2.1.5), has been chemically bound to Sepharose 4B and some of its properties have been studied. The optimal conditions for binding have been determined. The immobilized enzyme retained 48% of the activity of the soluble enzyme and the coupling yield amounted to 50%. Sepharose · succinyl CoA synthetase can be stored at 4°C for periods up to 90 days with only 25% loss of activity; it can also be repeatedly used without alteration of its enzymic activity. The complex showed enhanced thermal stability; pH optimum was between 7.0 and 8.0 for the bound enzyme, and 8.0 for the free enzyme. A general decrease in the Michaelis-Menten constants for the different substrates of the insoluble enzyme, as compared with values obtained for the free enzyme, was found. Plots of the rate product formation against ATP concentration changed from sigmoideal for the soluble succinyl CoA synthetase to hyperbolic for the immobilized enzyme. © 1978. |
| format |
JOUR |
| author |
Wider de Xifra, E.A. Batlle, A.M.D.C. |
| author_facet |
Wider de Xifra, E.A. Batlle, A.M.D.C. |
| author_sort |
Wider de Xifra, E.A. |
| title |
Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| title_short |
Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| title_full |
Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| title_fullStr |
Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| title_full_unstemmed |
Porphyrin biosynthesis: Immobilized enzymes and ligands VI. Studies on succinyl CoA synthetase from cultured soya bean cells |
| title_sort |
porphyrin biosynthesis: immobilized enzymes and ligands vi. studies on succinyl coa synthetase from cultured soya bean cells |
| url |
http://hdl.handle.net/20.500.12110/paper_00052744_v523_n1_p245_WiderdeXifra |
| work_keys_str_mv |
AT widerdexifraea porphyrinbiosynthesisimmobilizedenzymesandligandsvistudiesonsuccinylcoasynthetasefromculturedsoyabeancells AT batlleamdc porphyrinbiosynthesisimmobilizedenzymesandligandsvistudiesonsuccinylcoasynthetasefromculturedsoyabeancells |
| _version_ |
1782026681951715328 |