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Copper transport in rats involving a new plasma protein

Journal Article · · Am. J. Physiol.; (United States)
OSTI ID:5179550
The time course of distribution of high-specific activity /sup 67/CuCl/sub 2/ to tissues and plasma components was followed in adult, female rats. Immediately after intubation or injection, tracer /sup 67/Cu associated with two components of the blood plasma separable on columns of Sephadex G-150: albumin and another (larger) component, which was not ceruloplasmin. The latter, tentatively named transcuprein, had an apparent molecular weight of 270,000 and a high affinity for Cu2+, as judged by processing through Chelex-100, dilution, and exchange with albumin copper, in vitro and in vivo. It was capable of donating copper to tumor cells in serum-free medium. Analysis of ''cold'' plasma by furnace atomic absorption confirmed the presence of 10-15% of plasma copper in this peak. Plots of percent dose and /sup 67/Cu specific activity against time showed that copper followed a very specific pathway after binding to albumin and transcuprein, entering mainly the liver, then reappearing in the plasma on ceruloplasmin, and then achieving peak distribution in peripheral tissues (muscles, brain, etc.). /sup 67/Cu disappeared from liver and kidney with an apparent half-life of 4.5 days, the same exponential rate found for whole body turnover. Apparent turnover of ceruloplasmin copper was more rapid. Even after 7-12 days, tracer copper in plasma was still found exclusively with ceruloplasmin. The results indicate that copper follows a carefully prescribed path, on entering the blood and binding to a new transport protein.
Research Organization:
California State Univ., Fullerton
OSTI ID:
5179550
Journal Information:
Am. J. Physiol.; (United States), Journal Name: Am. J. Physiol.; (United States); ISSN AJPHA
Country of Publication:
United States
Language:
English