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Bilirubin attenuates radical-mediated damage to serum albumin

FEBS letters, 1993-10, Vol.331 (3), p.281-284 [Peer Reviewed Journal]

1993 ;FEBS Letters 331 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies ;1994 INIST-CNRS ;ISSN: 0014-5793 ;EISSN: 1873-3468 ;DOI: 10.1016/0014-5793(93)80353-V ;PMID: 8375511 ;CODEN: FEBLAL

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Title:
Bilirubin attenuates radical-mediated damage to serum albumin
Author: Neužil, Jiří ; Stocker, Roland
Subjects: Analytical, structural and metabolic biochemistry ; Antioxidant ; Antioxidants ; Ascorbate ; Bilirubin - physiology ; Biological and medical sciences ; BR, bilirubin ; BSA, bovine serum albumin ; BV, biliverdin ; Free Radicals ; Fundamental and applied biological sciences. Psychology ; Gamma Rays ; Heterocyclic compounds, pigments ; HO2, hydroperoxyl radical ; Irradiation ; Kyn, kynurenine ; Kynurenine ; Molecular biophysics ; OH, hydroxyl radical ; Other biological molecules ; Oxidation-Reduction ; O−. 2, Superoxide anion radical ; Protein oxidation ; Radiation-biomolecule interaction ; Radiochemistry ; ROS, reactive oxygen species ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - radiation effects ; Tetrapyrrolic pigments ; Trp, tryptophan ; Vitamin E
Is Part Of: FEBS letters, 1993-10, Vol.331 (3), p.281-284
Description: Oxidative damage to biological macromolecules has been implicated in a number of diseases. Much interest has focused on how non-proteinaceous, low-molecular weight antioxidants prevent oxidative damage to lipids, while comparatively little is known about protein antioxidation. Here we show that bilirubin (BR), the end-product of heme catabolism, when bound to bovine serum albumin (BSA), is oxidised by hydroxyl ('OH), hydroperoxyl (HO 2), and Superoxide anion (O xxx 2) radicals to so far mostly uncharacterised products. The initial oxidation rates of BSA-bound BR decreased in the order OH ⪢ HO 2 ⪢ O −. 2 BR protected its carrier protein from oxidative damage inflicted by OH radicals. This protective action included a reduction in the OH-mediated cleavage of BSA, conversion of Trp into kynurenine and formation of ‘bityrosine-specific’ fluorescence. BR also strongly inhibited OH-mediated formation of protein carbonyls, whereas ascorbate and Trolox (a water-soluble analogue of vitamin E) were much less effective. These results support an antioxidant-protective function of BR and point towards significant differences in the efficacies of various antioxidants in the prevention of oxidative damage to lipids and proteins.
Publisher: Amsterdam: Elsevier B.V
Language: English
Identifier: ISSN: 0014-5793
EISSN: 1873-3468
DOI: 10.1016/0014-5793(93)80353-V
PMID: 8375511
CODEN: FEBLAL
Source: Geneva Foundation Free Medical Journals at publisher websites
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Bilirubin attenuates radical-mediated damage to serum albumin

1993 ;FEBS Letters 331 (1993) 1873-3468 © 2015 Federation of European Biochemical Societies ;1994 INIST-CNRS ;ISSN: 0014-5793 ;EISSN: 1873-3468 ;DOI: 10.1016/0014-5793(93)80353-V ;PMID: 8375511 ;CODEN: FEBLAL

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