| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8333909 | International Journal of Biological Macromolecules | 2013 | 10 Pages |
Abstract
⺠DSC data show that HbGp unfolding is partially reversible at pH 7.0. ⺠AUC data show HbGp remains undissociated at 50 °C, fully dissociating above 60 °C. ⺠HbGp unfolding in neutral pH 7.0 is accompanied by aggregation, monitored by DLS. ⺠Protein concentration and temperature are critical in aggregation rate determination. ⺠HbGp is more stable in acidic medium than neutral solution, as it is shown by DSC and spectroscopy.
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Authors
José Wilson P. Carvalho, Francisco A.O. Carvalho, PatrÃcia S. Santiago, Marcel Tabak,