|
|
||||||||
Clinical Chemistry, Vol 13, 142-150, Copyright © 1967 by the American Association for Clinical Chemistry
1 Department of Chemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, Fla. 32306.
2 Institute for Medical Biochemistry, University of Oslo, Oslo, Norway.
A sensitive method for the detection of ceruloplasmin (ferroxidase) in human serums, using Fe(II) as the substrate, is described. Initial Fe(II) concentrations of 30 and 120 µM may be used, depending on the sensitivity of the spectrophotometer, for the determination of the rate of Fe(III) -transferrin formation following the oxidation of Fe(II) by ceruloplasmin (ferroxidase). Advantages of this method over other methods employing p-phenylenediamine as a substrate and the standardization of enzyme activity in terms of international enzyme units are discussed.
Submitted on April 5, 1966
The following articles in journals at HighWire Press have cited this article:
![]() |
J. Sarkar, V. Seshadri, N. A. Tripoulas, M. E. Ketterer, and P. L. Fox Role of Ceruloplasmin in Macrophage Iron Efflux during Hypoxia J. Biol. Chem., November 7, 2003; 278(45): 44018 - 44024. [Abstract] [Full Text] [PDF] |
||||
![]() |
K Hirano, T Morinobu, H Kim, M Hiroi, R Ban, S Ogawa, H Ogihara, H Tamai, and T Ogihara Blood transfusion increases radical promoting non-transferrin bound iron in preterm infants Arch. Dis. Child. Fetal Neonatal Ed., May 1, 2001; 84(3): 188F - 193. [Abstract] [Full Text] |
||||
![]() |
C. K. Mukhopadhyay, B. Mazumder, and P. L. Fox Role of Hypoxia-inducible Factor-1 in Transcriptional Activation of Ceruloplasmin by Iron Deficiency J. Biol. Chem., July 7, 2000; 275(28): 21048 - 21054. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |