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KMID : 1134819980270020305
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Journal of the Korean Society of Food Science and Nutrition
1998 Volume.27 No. 2 p.305 ~ p.312
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The Effect of Ascorbic Acid on the Enzyme Reaction in Pyridinoline Formation during Soluble Collagen Maturation
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Kim Mi-Hyang
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Abstract
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Normal tensile strength in collagen fibrils is due to intermolecular and intramolecular crosslinks which are known to be altered in aging. Pyridinoline, a mature crosslink which is stable and nonreducible, is derived from two hydroxyallysine and one hydroxy lysine residues of collagen fibrils. The excess formation of pyridinoline in collagen is associated with making the tissue stiffer, less soluble and less digestible by enzymes. Lysyl oxidase is the enzyme that initiates the biosynthesis of crosslinks in collagen by catalyzing the oxidative deamination of the lysyl and hydroxylysyl residues in these molecules, and its activity is inhibited by β-aminopropionitrile(BAPN). Our previous work demonstrated that the pyridinoline content of bone collagen significantly was increased during incubation for 5 weeks at 37℃ in vitro, but it was decreased by the addition of ascorbic acdi(AsA). In this study, we clarified the specific action of AsA in aging process in vitro enzymatic reaction.
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KEYWORD
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collagen, crosslink, pyridinoline, lysyl oxidase, AsA, BAPN
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