Bioscience Reports

, Volume 2, Issue 3, pp 169–175

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

  • K. K. Mäkinen
  • P. -L. Mäkinen

DOI: 10.1007/BF01116380

Cite this article as:
Mäkinen, K.K. & Mäkinen, P.L. Biosci Rep (1982) 2: 169. doi:10.1007/BF01116380


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.

Copyright information

© The Biochemical Society 1982

Authors and Affiliations

  • K. K. Mäkinen
    • 1
  • P. -L. Mäkinen
    • 2
  1. 1.Department of Biochemistry, Institute of DentistryUniversity of TurkuTurku 52Finland
  2. 2.Department of Forensic MedicineUniversity of TurkuTurku 50Finland

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