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The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake.
Proc Natl Acad Sci U S A
March 1995
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
The CCC2 gene of the yeast Saccharomyces cerevisiae is homologous to the human genes defective in Wilson disease and Menkes disease. A biochemical hallmark of these diseases is a deficiency of copper in ceruloplasmin and other copper proteins found in extracytosolic compartments. Here we demonstrate that disruption of the yeast CCC2 gene results in defects in respiration and iron uptake.
View Article and Find Full Text PDFStudies of copper transport in cultured bovine chondrocytes.
Biochim Biophys Acta
September 1994
Department of Medicine, Indiana University School of Medicine, Indianapolis 46202-5103.
Copper serves as the cofactor for a number of important enzymes in cartilage, as well as in other tissues, including lysyl oxidase, superoxide dismutase, and cytochrome oxidase. Ceruloplasmin is responsible for the transport of approx. 95% of the copper in serum, but the mechanisms for intracellular copper transport are unknown.
View Article and Find Full Text PDFPlasma ceruloplasmin. Evidence for its presence in and uptake by heart and other organs of the rat.
Biochim Biophys Acta
October 1977
Evidence for the presence of the plasma protein, ceruloplasmin, in heart and other tissues of the rat was sought using various techniques. With p-phenylenediamine, ceruloplasmin-like oxidase activity was detected in heart post-mitochondrial and 100 000 X g supernatants in amounts far exceeding those that could be accounted for by residual blood. Much lower levels were detected in kidney, brain and liver.
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