NDLI: Effect of Micronutrients on Methylglyoxal-Mediated In Vitro Glycation of Albumin

Content Provider	Springer Nature Link
Author	Tarwadi, Kirtan V. Agte, Vaishali V.
Copyright Year	2010
Abstract	Nonenzymatic glycation of long-lived proteins has been implicated in several complications related to age and diabetes. Dicarbonyl compounds such as methylglyoxal (MGO) have been identified as the predominant source for the formation of advanced glycation end-products (AGEs) in various tissues. We investigated the effect of 13 micronutrients on MGO-mediated in vitro glycation of bovine serum albumin (BSA), as formation of AGEs and protein carbonyls. BSA (10 mg/ml) was incubated at 37°C with 100 mM MGO for 24 hours, in presence of ascorbic acid, Trolox (water-soluble α-tocopherol analog), β-carotene, retinol, riboflavin, thiamin, folic acid, niacin, pyridoxine, zinc, iron, manganese, and selenium. Fluorescence was measured at the wavelength pair of 370 and 440 nm as an index of the formation of AGEs and spectra were recorded for promising interactions at λex = 280 nm and λex = 370 nm. Within four standard antiglycating agents, aminoguanidine showed highest inhibitory response for BSA glycation followed by quercetin, gallic acid, and tannic acid. Promising antiglycation potential was seen for Trolox, riboflavin, Zn, and Mn as evidenced by decrease in the formation of AGEs and protein carbonyls.
Starting Page	717
Ending Page	725
Page Count	9
File Format	PDF
ISSN	01634984
Journal	Biological Trace Element Research
Volume Number	143
Issue Number	2
e-ISSN	15590720
Language	English
Publisher	Humana Press Inc
Publisher Date	2010-12-17
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	BSA Methylglyoxal Nonenzymatic glycation AGE Protein carbonyls Oncology Biotechnology Biochemistry Nutrition
Content Type	Text
Resource Type	Article
Subject	Biochemistry (medical) Endocrinology, Diabetes and Metabolism Clinical Biochemistry Biochemistry Inorganic Chemistry

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