Photolysis of pyridinoline, a cross-linking amino acid of collagen, by ultraviolet light.

S Sakura, D Fujimoto, K Sakamoto, A Mizuno, K Motegi
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引用次数: 46

Abstract

Pyridinoline, a cross-linking amino acid of collagen, was degraded by irradiation of ultraviolet light. The decomposition rate varied with pH of the solution and wavelength of irradiation light. The maximum of the degradation rate at individual pH coincides with the ultraviolet absorption maximum. Namely, it was maximally degraded by irradiation at 295 nm in acidic solution and at 325 nm in neutral and alkaline solution. At the optimum wavelength, the photolysis occurred more rapidly in neutral and alkaline solution than in acidic solution. The quantum yield in neutral solution was approximately 0.11 and independent of wavelength. One of the photolysis products was identified as hydroxylysine on an amino acid analyser, indicating that the cleavage of the pyridinium ring occurred.

用紫外线光解吡啶啉,胶原蛋白的一种交联氨基酸。
对胶原交联氨基酸吡啶啉进行了紫外光照射降解。分解速率随溶液pH和照射光波长的变化而变化。各pH值下的降解速率最大值与紫外吸收最大值一致。即在酸性溶液中辐照295 nm,在中性和碱性溶液中辐照325 nm时降解效果最好。在最佳波长下,中性和碱性溶液中的光解反应速度快于酸性溶液。中性溶液中的量子产率约为0.11,与波长无关。其中一个光解产物在氨基酸分析仪上被鉴定为羟基赖氨酸,表明发生了吡啶环的裂解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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