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 l-phenyl-l,2-propanedione. Methylglyoxal caused similar effects at 25zt nm. 2-Thiol-L-histidine and 3-methyl-L-histidine protected the enzymes against photoinactivation more effectively than N3−, even at a molar ratio of 2:1 (protector to enzyme). These compounds also delayed the photoinactivation of acetylcholinesterase, induced by ultraviolet light.
Oxidation, photosensitized by certain diketones, of enzymes and protection against such oxidation by histidine derivatives
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K. K. Mäkinen, P.-L. Mäkinen; Oxidation, photosensitized by certain diketones, of enzymes and protection against such oxidation by histidine derivatives. Biosci Rep 1 March 1982; 2 (3): 169–175. doi: https://doi.org/10.1007/BF01116380
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