Effect of cadmium on ceruloplasmin levels in the rat Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/x633f3351

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  • Injection of a 2.0 mg Cd ²⁺ /kg B.W. (I.P. as CdC1 ₂ in .05 M NaAc, pH = 6.9-7.2, .15 M or p = .15 with NaCl) resulted in a decrease in ceruloplasmin (EC 1.12.3) p-phenylenediamine oxidase activity within one hour of injection. Maximal decrease (40%) occurred within six to eight hours, with levels rising slowly over the duration of the experiment (28.5 hours postinjection). Cadmium-109 (36 pCi carrier free ¹⁰⁹ CdC1 ₂ in .05 M HC1, .15 M NaC1) was injected (I.P.) into rats and plasma obtained five hours later. Purification of the ceruloplasmin using DEAE and Sephadex G-200 chromatography revealed significant cadmium-109 in the ceruloplasmin fraction. In vitro binding was not observed. Attempts were made to purify ceruloplasmin utilizing, DEAE, hydroxylapatite and Sephadex G-200 chromatography coupled with ethanol-chloroform precipitation. The product obtained was spectrophotometrically pure and deemed electrophoretically homogeneous, however antibody produced in rabbits to this antigen was not homogeneous as revealed by immunoelectrophoresis and Ouchterlony immunodiffusion. The precipitin response of the antiserum obtained was investigated with respect to the effect of dilution, pH and NaC1 concentration. The equivalence point was shown to remain essentially independent of dilution (over a range of 1.3 to 10), pH (from 5.8 to 8.0) or NaC1 concentration (.01 M to .25 M). The point of maximal protein precipitation was affected by pH and the amount of protein precipitated was decreased by dilution and unaffected by changing salt concentration. The experiments involving cadmium suggest the mechanism of cadmium induced inhibition of ceruloplasmin oxidase activity does not involve decreased synthesis. The in vivo binding of cadmium to ceruloplasmin may be the cause of decreased oxidase activity.
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