Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins.
Grape thaumatin-like (TL) proteins and chitinases play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. A two-step method is described that highly purified hundreds of milligrams of TL proteins and chitinases from two juices by strong ca...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2009
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| _version_ | 1797065773512916992 |
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| author | Van Sluyter, S Marangon, M Stranks, S Neilson, K Hayasaka, Y Haynes, P Menz, R Waters, E |
| author_facet | Van Sluyter, S Marangon, M Stranks, S Neilson, K Hayasaka, Y Haynes, P Menz, R Waters, E |
| author_sort | Van Sluyter, S |
| collection | OXFORD |
| description | Grape thaumatin-like (TL) proteins and chitinases play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. A two-step method is described that highly purified hundreds of milligrams of TL proteins and chitinases from two juices by strong cation exchange (SCX) and hydrophobic interaction chromatography (HIC). The method was fast and separated isoforms of TL proteins and chitinases from within the same juice, in most cases to >97% purity. The isolated proteins were identified by peptide nanoLC-MS/MS and crystallized using a high-throughput screening method. Crystals from three protein fractions produced high-resolution X-ray crystallography data. |
| first_indexed | 2024-03-06T21:33:23Z |
| format | Journal article |
| id | oxford-uuid:456c5312-d1e9-4b57-83ca-8abf41f48acf |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:33:23Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:456c5312-d1e9-4b57-83ca-8abf41f48acf2022-03-26T15:07:45ZTwo-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:456c5312-d1e9-4b57-83ca-8abf41f48acfEnglishSymplectic Elements at Oxford2009Van Sluyter, SMarangon, MStranks, SNeilson, KHayasaka, YHaynes, PMenz, RWaters, EGrape thaumatin-like (TL) proteins and chitinases play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. A two-step method is described that highly purified hundreds of milligrams of TL proteins and chitinases from two juices by strong cation exchange (SCX) and hydrophobic interaction chromatography (HIC). The method was fast and separated isoforms of TL proteins and chitinases from within the same juice, in most cases to >97% purity. The isolated proteins were identified by peptide nanoLC-MS/MS and crystallized using a high-throughput screening method. Crystals from three protein fractions produced high-resolution X-ray crystallography data. |
| spellingShingle | Van Sluyter, S Marangon, M Stranks, S Neilson, K Hayasaka, Y Haynes, P Menz, R Waters, E Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title | Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title_full | Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title_fullStr | Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title_full_unstemmed | Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title_short | Two-step purification of pathogenesis-related proteins from grape juice and crystallization of thaumatin-like proteins. |
| title_sort | two step purification of pathogenesis related proteins from grape juice and crystallization of thaumatin like proteins |
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