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紫外线对吡啶啉(一种胶原蛋白的交联氨基酸)的光解作用。

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

作者信息

Sakura S, Fujimoto D, Sakamoto K, Mizuno A, Motegi K

出版信息

Can J Biochem. 1982 May;60(5):525-9. doi: 10.1139/o82-064.

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.

摘要

吡啶啉是胶原蛋白的一种交联氨基酸,经紫外线照射会发生降解。分解速率随溶液的pH值和照射光的波长而变化。在各个pH值下,降解速率的最大值与紫外线吸收最大值一致。也就是说,在酸性溶液中,295nm波长的照射使其降解程度最大;在中性和碱性溶液中,325nm波长的照射使其降解程度最大。在最佳波长下,光解在中性和碱性溶液中比在酸性溶液中发生得更快。中性溶液中的量子产率约为0.11,且与波长无关。在氨基酸分析仪上,其中一种光解产物被鉴定为羟赖氨酸,这表明吡啶环发生了裂解。

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