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Kinetin Inhibits Protein Oxidation and Glycoxidation in Vitro

We tested the ability of N6-furfuryladenine (kinetin) to protect against oxidative and glycoxidative protein damage generated in vitro by sugars and by an iron/ascorbate system. At 50 μM, kinetin was more efficient (82% inhibition) than adenine (49% inhibition) to inhibit the bovine serum albumin (B...

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Published in:Biochemical and biophysical research communications 2000-10, Vol.276 (3), p.1265-1270
Main Authors: Verbeke, Philippe, Siboska, Gunhild E., Clark, Brian F.C., Rattan, Suresh I.S.
Format: Article
Language:English
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Summary:We tested the ability of N6-furfuryladenine (kinetin) to protect against oxidative and glycoxidative protein damage generated in vitro by sugars and by an iron/ascorbate system. At 50 μM, kinetin was more efficient (82% inhibition) than adenine (49% inhibition) to inhibit the bovine serum albumin (BSA)-pentosidine formation in slow and fast glycation/glycoxidation models. Kinetin also inhibited the formation of BSA-carbonyls after oxidation significantly more than adenine did. However both compounds inhibited the advanced glycation end product (AGE) formation to the same extent (59–68% inhibition). At 200 μM, kinetin but not adenine, limited the aggregation of BSA during glycation. These data suggest that kinetin is a strong inhibitor of oxidative and glycoxidative protein-damage generated in vitro.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.3616