Literature DB >> 996846

Effects of copper deficiency and copper loading on 67Cu in supernatants of rat organs.

T Terao, C A Owen.   

Abstract

Eleven organs of the rat were studied 1 hr and 24 hr after the intravenous administration of 67CuCl2 and 67Cu-ceruloplasmin. The rats were normal, copper-deficient, or copper-laden. The amounts of stable copper and 67Cu in the whole organ and supernatant fractions, corrected for whole blood copper and 67Cu, were measured. The distribution of supernatant 67Cu was determined in three Sephadex G-100 chromatographic zones: Peak I (150,000 daltons), Peak II (31,000 daltons), and Peak III (11,000 daltons). All organs took up 67Cu from both sources, but there was a tendency for increased uptakes in copper-deficient rats and decreased uptake in copper-laden rats. Only lung, heart, and testis took up more 67Cu from 67Cu-ceruloplasmin than from 67CuCl2. Supernatant 67Cu tended to be in Peak I when the source was 67Cu-ceruloplasmin and in Peak II when the source was 67CuCl2. When 67Cu-ceroloplasmin was added to supernatant fractions in vitro, the 67Cu was in Peak I. However, when 67CuCl2 was added to supernatant fractions, Peak III predominated in kidney, brain, testis, and liver; Peak II predominated in none; and Peak I predominated in spleen, muscle, large and small bowel, stomach, lung, and heart. A high-molecular-weight copper-binding substance seems to be present in organ supernatant fractions.

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Year:  1976        PMID: 996846     DOI: 10.1620/tjem.120.209

Source DB:  PubMed          Journal:  Tohoku J Exp Med        ISSN: 0040-8727            Impact factor:   1.848


  5 in total

1.  Comparison of pathways of copper metabolism in aorta and liver. A functional test of metallothionein.

Authors:  J E Balthrop; C T Dameron; E D Harris
Journal:  Biochem J       Date:  1982-05-15       Impact factor: 3.857

2.  Cytosolic copper-binding proteins in rat and mouse hepatocytes incubated continuously with Cu(II).

Authors:  F A Palida; A Mas; L Arola; K Bethin; P A Lonergan; M J Ettinger
Journal:  Biochem J       Date:  1990-06-01       Impact factor: 3.857

3.  Regulation of aortic CuZn-superoxide dismutase with copper. Caeruloplasmin and albumin re-activate and transfer copper to the enzyme in culture.

Authors:  C T Dameron; E D Harris
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

4.  In vitro assessment of the toxicity of metal compounds : IV. Disposition of metals in cells: Interactions with membranes, glutathione, metallothionein, and DNA.

Authors:  N T Christie; M Costa
Journal:  Biol Trace Elem Res       Date:  1984-04       Impact factor: 3.738

5.  Relationship between ceruloplasmin and Cu status involving metallothionein induced by several heavy metals in the mouse.

Authors:  N Sugawara; C Sugawara
Journal:  Arch Toxicol       Date:  1987-04       Impact factor: 5.153

  5 in total

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