Abstract
The role of metal (especially) iron ions has been postulated to play a prominent role in protein glycation, suggesting antiglycating effectiveness of metal chelators. However, this rule may not apply to all model glycation systems. We found that metal chelators are not effective in prevention of glycation of bovine serum albumin (BSA) in vitro, and there is no correlation between the antiglycating effects of 32 compounds and their iron chelation activity as measured with the ferrozine test. These data indicate that the glycation of BSA in vitro is iron-independent and is not a proper system to study the role of metals in protein glycation.
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- Is Iron Chelation Important in Preventing Glycation of Bovine Serum Albumin in Vitro?
- The transition of the 37-kDa laminin receptor (RPSA) to higher molecular weight species: SUMOylation or artifact?
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- Bioinformatics-based molecular classification of Arthrobacter plasmids
- Ras Transformation Overrides a Proliferation Defect Induced by Tpm3.1 Knockout
- The advanced lipoxidation end product precursor malondialdehyde induces IL-17E expression and skews lymphocytes to the Th17 subset
- On Application of Langevin Dynamics in Logarithmic Potential to Model Ion Channel Gate Activity
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