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

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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 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.

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Authors and Affiliations

  1. Department of Biochemistry, Institute of Dentistry, University of Turku, SF-20520, Turku 52, Finland

    K. K. Mäkinen

  2. Department of Forensic Medicine, University of Turku, SF-20500, Turku 50, Finland

    P. -L. Mäkinen

Authors
  1. K. K. Mäkinen
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  2. P. -L. Mäkinen
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Mäkinen, K.K., Mäkinen, P.L. Oxidation, photosensitized by certain diketones, of enzymes and protection against such oxidation by histidine derivatives. Biosci Rep 2, 169–175 (1982). https://doi.org/10.1007/BF01116380

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  • DOI: https://doi.org/10.1007/BF01116380

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