Literature DB >> 523962

Kinetics of bilirubin oxidation with peroxidase, as applied to studies of bilirubin-albumin binding.

R Brodersen, W J Cashore, R P Wennberg, C E Ahlfors, L F Rasmussen, D Shusterman.   

Abstract

In the determination of unbound bilirubin by rate of oxidation with peroxidase, errors may be caused by (1) phenol, propylparaben, and phenothiazines (free radical acceleration), (2) haemoglobin (peroxidase effect), and (3) ascorbate (inhibition). Such errors may be diminished by dilution 1:40, or with an anti-oxidant, tert-butyl-p-hydroxyanisole, and ascorbate oxidase.

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Year:  1979        PMID: 523962     DOI: 10.1080/00365517909106086

Source DB:  PubMed          Journal:  Scand J Clin Lab Invest        ISSN: 0036-5513            Impact factor:   1.713


  2 in total

1.  Principles of a competitive binding assay for the study of the interactions of poorly water-soluble ligands with their soluble binding partners. Application to bilirubin with the use of Sephadex G-10 as a competitive adsorbent.

Authors:  J A Meuwissen; M Kinnaert; G Michiels; K P Heirwegh
Journal:  Biochem J       Date:  1988-01-01       Impact factor: 3.857

2.  The effect of bilirubin photoisomers on unbound-bilirubin concentrations estimated by the peroxidase method.

Authors:  S Itoh; T Yamakawa; S Onishi; K Isobe; M Manabe; K Sasaki
Journal:  Biochem J       Date:  1986-10-15       Impact factor: 3.857

  2 in total

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