Purification and characterization of chromium-binding substances from high-chromium yeast

As a highly efficient and easily absorbable source of chromium, the identities of the chromium-binding substances in yeast remain unclear. In this study, a mild extraction procedure involving extraction with ammonia, three-gel filtration, and high-performance liquid chromatography was adopted to obtain two chromium-binding substances from high-chromium yeast. A low-molecular-weight chromium-binding substance was identified, with mass-to-charge ratios (m/z) of 769 and 712, which included glutamic acid, glycine, and cysteine in an approximate ratio of 1:1:1, as well as nicotinic acid and chromium(III). Furthermore, it significantly potentiated (by 51%) the action of insulin to stimulate the conversion of (14)C-glucose into lipid in adipocytes. A novel high-molecular-weight chromium-binding substance was also isolated: electrospray ionization tandem mass spectrometry tentatively identified it as HUB1 target protein-1, glyceraldehyde-3-phosphate dehydrogenase, or ribosomal protein L2A(L5A)(rp8)(YL6). This is the first report of a high-molecular-weight chromium-binding substance in yeast and merits further studies.