Properties of the mercury and selenium complex formed in rat plasma in vivo.

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Abstract
Properties of the Hg and Se complex (Hg-Se complex) produced in plasma after the simultaneous injection of HgCl2 and Na2SeO3 were investigated by pronase digestion and isoelectric focusing. When the gel chromatographic fraction containing the Hg-Se complex was digested with Pronase E and chromatographed on a Sephadex G-200 column, the resulting derived proteins contained no Hg and little Se. Most Hg and Se in the digest of the Hg-Se complex remained at the top of the column, but the content of proteins (derived proteins) found at the same site of column was only trace amount. Derived proteins obtained from proteins containing Hg or Se in serum by the same digestion contained Hg and high percentage of Se, respectively. The Hg-Se complex in plasma did not contain protein as a component. When the isoelectric focusing of the serum containing the Hg-Se complex was done, the peak containing both Hg and Se was present in the position of pH 2 and 4. The former peak was independent of the serum proteins, the latter peak overlapped its distribution. Similar behavior of Hg and Se was observed in the isoelectric focusing of the mercuric selenide colloid dispersed in the solution containing bovine serum albumin. The properties of the Hg-Se complex supported the hypothesis that it was a mercuric selenide colloid.