ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING
abstract A procedure of isolation of oxalate oxidase from barley seedling and a new method for purification is described. A purification step was accomplished by the second partition using poly ethylene glycol (PEG-6000) and Devi-Iran-500 (4.5%1 4), and affinity chromatography using oxalate immobili...
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[Yogyakarta] : Universitas Gadjah Mada
1991
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| _version_ | 1797018253018529792 |
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| author | Perpustakaan UGM, i-lib |
| author_facet | Perpustakaan UGM, i-lib |
| author_sort | Perpustakaan UGM, i-lib |
| collection | UGM |
| description | abstract
A procedure of isolation of oxalate oxidase from barley seedling and a new method for purification is described.
A purification step was accomplished by the second partition using poly ethylene glycol (PEG-6000) and Devi-Iran-500 (4.5%1 4), and affinity chromatography using oxalate immobilized on activated CNBR-Sepharose 6MB as a ligand.
After partition some protein were separated, and the specific activity were increased by 5-30 fold. The affinity chromatography using Oxalate-Sepharose effectively separated the oxalate oxidase. The specific activity of pure enzyme was 154.3 U/mg protein and the purity was 41 fold.
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| first_indexed | 2024-03-05T22:57:49Z |
| format | Article |
| id | oai:generic.eprints.org:20472 |
| institution | Universiti Gadjah Mada |
| last_indexed | 2024-03-13T18:41:07Z |
| publishDate | 1991 |
| publisher | [Yogyakarta] : Universitas Gadjah Mada |
| record_format | dspace |
| spelling | oai:generic.eprints.org:204722014-06-18T00:41:09Z https://repository.ugm.ac.id/20472/ ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING Perpustakaan UGM, i-lib Jurnal i-lib UGM abstract A procedure of isolation of oxalate oxidase from barley seedling and a new method for purification is described. A purification step was accomplished by the second partition using poly ethylene glycol (PEG-6000) and Devi-Iran-500 (4.5%1 4), and affinity chromatography using oxalate immobilized on activated CNBR-Sepharose 6MB as a ligand. After partition some protein were separated, and the specific activity were increased by 5-30 fold. The affinity chromatography using Oxalate-Sepharose effectively separated the oxalate oxidase. The specific activity of pure enzyme was 154.3 U/mg protein and the purity was 41 fold. Introduction [Yogyakarta] : Universitas Gadjah Mada 1991 Article NonPeerReviewed Perpustakaan UGM, i-lib (1991) ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING. Jurnal i-lib UGM. http://i-lib.ugm.ac.id/jurnal/download.php?dataId=3323 |
| spellingShingle | Jurnal i-lib UGM Perpustakaan UGM, i-lib ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title | ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title_full | ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title_fullStr | ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title_full_unstemmed | ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title_short | ISOLATION AND PURIFICATION OF OXALATE OXIDASE FROM BARLEY SEEDLING |
| title_sort | isolation and purification of oxalate oxidase from barley seedling |
| topic | Jurnal i-lib UGM |
| work_keys_str_mv | AT perpustakaanugmilib isolationandpurificationofoxalateoxidasefrombarleyseedling |