Thermal Dissection of Lentil Seedling Amine Oxidase Domains by Differential Scanning Calorimetry
| Autor: | Faizan Ahmad, Anna Mura, Reza Yousefi, Ali Akbar Saboury, S. Hashemnia, Mojtaba Amani, Gholam Hossein Hakimelahi, Mostafa Rezaei-Tavirani, Ali Akbar Moosavi-Movahedi, Giovanni Floris, S.Z. Moosavi-Nejad |
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| Rok vydání: | 2007 |
| Předmět: |
Protein Denaturation
Amine oxidase Stereochemistry Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Differential scanning calorimetry Organic chemistry Denaturation (biochemistry) Thermal stability Molecular Biology chemistry.chemical_classification Oxidase test Calorimetry Differential Scanning biology Organic Chemistry Active site General Medicine Protein Structure Tertiary Enzyme chemistry Seedlings biology.protein Lens Plant Amine gas treating Amine Oxidase (Copper-Containing) Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 71:1644-1649 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | The relationships between the structural and energetic domains of lentil seedling amine oxidase (LSAO) were investigated using modifiers that target the active site and the carbohydrate moiety of the enzyme. An irreversible inhibitor, aminoguanidine, specifically modified the active site of the lentil enzyme, whereas sodium metaperiodate cleaves carbohydrate moieties covalently bound to the native enzyme. Differential scanning calorimetry (DSC) measurements were made on the modified LSAOs. Deconvolution of the reversible thermal DSC profiles of the modified enzyme gave three subpeaks (energetic domains), each of which was assigned to one of the three structural domains of the native protein. Our results led us to conclude that deglycosylation of LSAO has no effect on thermal stability, whereas binding of the inhibitor imparts more stability to the enzyme. |
| Databáze: | OpenAIRE |
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