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KMID : 0613820040140030478
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Journal of Life Science
2004 Volume.14 No. 3 p.478 ~ p.483
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The effect of L-Ascorbic Acid on the Oxidative Reaction of Lysine in Collagen
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Kim Mi-Hyang
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Abstract
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In a model reaction using lysyl oxidase purified partilally from bovine aorta, effect of L-ascorbic acid AsA on the oxidative reaction of lysine in collagen was investigated. Addition of AsA to the reaction mixture under aerobic conditions resulted in the decrease of enzymatic activity. In order to examine the specificity of AsA in the oxidative reaction of lysine, other reductants including AsA derivatives instead of AsA were added to the reaction mixture. Thiol such as glutathione had no effect on the activities of lysyl oxidase. on the other hand, it was observed that erythorbic acid, which was a stereoisomer of AsA, had the same inhibitory effect on this oxidative reaction as AsA. Moreover, by the addition of 3,4-dihydroxybenzoate, which was structural analog of AsA, the activities decreased in a similar manner to that of AsA. These results indicate that the regulatory effect of AsA on lysyl oxidase is attributed to characteristics of the structure. From the determination of AsA remained in the reaction mixture, it is shown that AsA concentration remarkably decreased by lysyl oxidase of the reaction mixture. It is hypothesized that endiol groups reduces the enzyme-bound Cu2+ required for further progress of the reaction, and suggests that AsA regulates specifically the reduction of Cu2+ required to oxidize lysyl oxidase. This findings support that AsA has an important regulatory role on the oxidative reaction of lysine and on changes of collagen cross-links with aging.
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KEYWORD
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AsA, lysine, lysyl oxidase, oxidative reaction
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