PMID: 1205450Nov 1, 1975Paper

Formation, circular dichroism and x-ray photoelectron spectroscopy of hepatic Zn-thionein

Hoppe-Seyler's Zeitschrift für physiologische Chemie
G Sokolowski, U Weser

Abstract

The formation of the powerful Zn binding protein called Zn-thionein was examined using male albino rats and [14C]cysteine, as cystein is known to be the most abundant constituent of this metal protein. 65% of the hepatic [14C]cysteine was incorporated into the protein portion of freshly prepared Zn-thionein. The protein was isolated by a combination of ethanol/chloroform treatment and various chromatographic steps, including ion exchange and gel filtration. 4.7 mol of Zn, 0.02 mol of Cd and less than 0.001 mol of either Cu or Hg were found per 12 000 g of portein. It was presumed that considerable amounts of Zn were lost during these isolation procedures, with the consequence of disulphide gridge formation. Indeed, the presence of R-S-S-R was deduced from circular dichroism and X-ray photoelectron spectroscopy. Due to the clearly detectable disulphide chromophore in the circular dichroism spectrum, it was possible to assign the shoulder at S 2p1/2,3/2 = 162.7 eV of the X-ray photoelectron spectrum of native Zn-thionein to R-S-S-R and not to strongly polarized sulphur. Upon reducing R-S-S-R-containing native Zn-thionein with dithiothreitol, all oxidised thiolate moieties of the thionein molecule could be restored. The addition o...Continue Reading

Citations

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