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Ferrous oxidase ceruloplasmin assay

Salim Neselioglu, Merve Ergin, Ozcan Erel
A new kinetic and automated assay was developed to determine ceruloplasmin ferroxidase activity. Ferrous ions are turned into ferric ions via catalytic activity of the ferroxidase enzyme. Acetohydroxamic acid, a chromogen, forms a colored complex with ferric ions. This reaction was measured kinetically. Significant and strong correlations were obtained between the new acetohydroxamic method and the p-phenylenediamine oxidase (r = 0.988, p <0.001), o-dianisidine oxidase (r = 0.981, p <0.001), norfloxacine oxidase (r = 0...
2017: Analytical Sciences: the International Journal of the Japan Society for Analytical Chemistry
Laura Cortes, Blaine R Roberts, Anthony G Wedd, Zhiguang Xiao
Ceruloplasmin (Cp) is one of the most complex multicopper oxidase enzymes and plays an essential role in the metabolism of iron in mammals. Ferrous ion supplied by the ferroportin exporter is converted by Cp to ferric ion that is accepted by plasma metallo-chaperone transferrin. Study of the enzyme at the atomic and molecular level has been hampered by the lack of a suitable ferrous substrate. We have developed the classic chromophoric complex FeII Hx (Tar)2 (H2 Tar, 4-(2-thiazolylazo)resorcinol; x = 0-2; overall charge omitted) as a robust substrate for evaluation of the ferroxidase function of Cp and related enzymes...
May 1, 2017: Inorganic Chemistry
K B Male, J H Luong
1,1'-dimethylferricinium (DMFe+), a stable and pH-insensitive blue dye, was prepared via enzymatic oxidation of a 1,1'dimethyl-ferrocene (DMFe):2-hydroxypropyl-beta-cyclodextrin (HPCD) water-soluble inclusion complex, using bilirubin oxidase immobilized onto porous aminopropyl glass beads via glutaraldehyde activation. In the presence of glucose, DMFe+ was reduced to DMFe by reacting with the reduced glucose oxidase (FADH2), and the absorbance decrease was followed at 650 nm. In acetate pH 5.2 buffer, the response to glucose in blood serum was nonlinear, especially in the low concentration range, because of a competition for the reduced glucose oxidase between the DMFe+ dye and oxygen...
December 1996: Applied Biochemistry and Biotechnology
C Askwith, D Eide, A Van Ho, P S Bernard, L Li, S Davis-Kaplan, D M Sipe, J Kaplan
S. cerevisiae accumulate iron by a process requiring a ferrireductase and a ferrous transporter. We have isolated a mutant, fet3, defective for high affinity Fe(II) uptake. The wild-type FET3 gene was isolated by complementation of the mutant defect. Sequence analysis of the gene revealed the presence of an open reading frame coding for a protein with strong similarity to the family of blue multicopper oxidoreductases. Consistent with the role of copper in iron transport, growth of wild-type cells in copper-deficient media resulted in decreased ferrous iron transport...
January 28, 1994: Cell
J Winkles, A F Jones, P Winyard, D R Blake, J Lunec
The oxidase activity of caeruloplasmin towards Fe II (ferroxidase) appears to be of physiological significance both in iron metabolism and as a serum anti-oxidant. We have developed an automated assay for ferroxidase using a centrifugal analyser. The method is quick and precise, and is not subject to interference by haemolysis, jaundice or lipaemia. Ferroxidase activities correlate significantly with caeruloplasmin and copper concentrations. Normal reference ranges have been measured.
May 1988: Annals of Clinical Biochemistry
J M Gutteridge
Multifunctional roles of the plasma protein, caeruloplasmin, have been briefly reviewed under three main headings. These are protein functions, enzymic activity, and antioxidant protection. As a plasma protein it is said to play a role in the transport of copper. Since some 95% of serum copper is associated with caeruloplasmin, measurement of the protein provides a useful guide to copper levels. Enzymic functions are related to its oxidase activity. Substrates commonly used for laboratory assay include non-biologically occurring aromatic amines and polyphenols...
November 1978: Annals of Clinical Biochemistry
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