Effects of in vitro glycation on Fe3+ binding and Fe3+ isoforms of transferrin104

Last updated on 22-8-2019 by Anonymous (niet gecontroleerd)

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Peer reviewed scientific article


BACKGROUND: In diabetes, protein function is altered by glycation, but the impact on the Fe3+ binding and antioxidant functions of transferrin (Tf) is largely unknown. The aim of the present study was to investigate the effects of glycation on the distribution of Fe3+ on the two Fe3+ -binding sites of Tf. METHODS: In vitro glycation of Tf was accomplished by preincubation with glucose for 14 days. Tf was loaded with Fe3+ compounds to achieve theoretical Tf Fe3+ saturations of 32%, 64%, and 96% (monitored by spectrophotometry). Fe3+ -Tf isoforms were separated by isoelectric focusing. RESULT

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