某些二酮光敏化引起的酶的氧化以及组氨酸衍生物对这种氧化的防护作用。

Oxidation, photosensitized by certain diketones, of enzymes and protection against such oxidation by histidine derivatives.

作者信息

Mäkinen K K, Mäkinen P L

出版信息

Biosci Rep. 1982 Mar;2(3):169-75. doi: 10.1007/BF01116380.

Abstract

Bovine milk lactoperoxidase, eel acetylcholinesterase, and Aeromonas aminopeptidase were photooxidized and inactivated in broad-spectrum visible light in the presence of 2,3-butanedione and 1-phenyl-1,2-propanedione. Methylglyoxal caused similar effects at 254 nm. 2-Thiol-L-histidine and 3-methyl-L-histidine protected the enzymes against photoinactivation more effectively then N3-, even at a molar ratio of 2:1 (protector to enzyme). These compounds also delayed the photoinactivation of acetylcholinesterase, induced by ultraviolet light.

摘要

牛乳中的乳过氧化物酶、鳗鱼的乙酰胆碱酯酶以及气单胞菌氨肽酶在2,3 -丁二酮和1 -苯基-1,2 -丙二酮存在的情况下，于广谱可见光下发生光氧化并失活。甲基乙二醛在254纳米处产生类似效果。2 -硫醇-L -组氨酸和3 -甲基-L -组氨酸比N3 -更有效地保护这些酶免受光灭活，即使在摩尔比为2:1（保护剂与酶）时也是如此。这些化合物还延缓了紫外线诱导的乙酰胆碱酯酶的光灭活。