Molten globule of hemoglobin proceeds into aggregates and advanced glycated end products.
Conformational alterations of bovine hemoglobin (Hb) upon sequential addition of glyoxal over a range of 0-90% v/v were investigated. At 20% v/v glyoxal, molten globule (MG) state of Hb was observed by altered tryptophan fluorescence, high ANS binding, existence of intact heme, native-like secondary...
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| Autors principals: | , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Public Library of Science (PLoS)
2013-01-01
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| Col·lecció: | PLoS ONE |
| Accés en línia: | http://europepmc.org/articles/PMC3753358?pdf=render |
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