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

R. Brodersen Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

W. J. Cashore Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

R. P. Wennberg Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

C. E. Ahlfors Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

L. F. Rasmussen Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

D. Shusterman Institute of Medical Biochemistry, University of Århus, DK-8000, Århus C, Denmark; Women and Infants Hospital of Rhode Island, Brown University, Providence, Rhode, Island; Department of Pediatrics, Sacramento Medical Center, University of California, Davis, Sacramento, California, 95817, USA

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 antioxidant, tert-butyl-p-hydroxyanisole, and ascorbate oxidase.

Key Words:

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

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

Information for

Open access

Opportunities

Help and information

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

Abstract

Reprints and Corporate Permissions

Academic Permissions

Related research

To cite this article:

Download citation

Information for

Open access

Opportunities

Help and information

Keep up to date

Your download is now in progress and you may close this window

Login or register to access this feature