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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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Bibliografische Detailangaben
Hauptverfasser: Afshin Iram, Tauqeer Alam, Javed M Khan, Taqi A Khan, Rizwan H Khan, Aabgeena Naeem
Format: Artigo
Sprache:Inglês
Veröffentlicht: Public Library of Science (PLoS) 2013-01-01
Schriftenreihe:PLoS ONE
Online-Zugang:http://europepmc.org/articles/PMC3753358?pdf=render
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