Abstract
A butanol: H 2O extract of Brewers' yeast grown in a medium which contained 51Cr was analyzed by gel-filtration chromatography. A single radioactive peak was eluted at an elution volume which suggested a molecular weight of approximately 400–600 daltons. Subsequent examination of pooled radioactive fractions obtained from gel-filtration chromatography demonstrated that the 51Cr complex was eluted in a single peak from both cation- and anion-exchange resins. The elution characteristics of the 51Cr complex indicated that the compound is a single anionic species. The 51Cr complex was purified by a combination of gel-filtration chromatography and ion-exchange chromatography and subsequently analyzed by thin-layer chromatography. The results indicated that the 51Cr complex from Brewers' yeast is a peptide that contains at least six amino acids. When a partially purified preparation of the 51Cr complex from yeast was administered orally to rats, the absorption and retention of 51Cr was significantly greater than that in rats given 51Cr in the form of CrCl 3·6H 2O. These experiments demonstrate that chromium is associated with a single metal-binding peptide in Brewers' yeast and indicate that the chromium in this complex is absorbed and retained more efficiently than chromium salts.
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