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

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-...

Full description

Saved in:
Bibliographic Details
Published inBioscience reports Vol. 2; no. 3; p. 169
Main Authors Mäkinen, K K, Mäkinen, P L
Format Journal Article
LanguageEnglish
Published England 01.03.1982
Subjects
Acetylcholinesterase - radiation effects
Aminopeptidases - radiation effects
Animals
Cattle
Diacetyl - pharmacology
Histidine - analogs & derivatives
Histidine - pharmacology
Lactoperoxidase - radiation effects
Light
Methylhistidines - pharmacology
Oxidation-Reduction
Peroxidases - radiation effects
Pyruvaldehyde - pharmacology
Ultraviolet Rays
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0144-8463
DOI:10.1007/BF01116380