Separation of polythiolate peptides and metallopeptides by covalent affinity chromatography

Summary Metallothionein (MT) a low-molecular weight polythiolate metallopeptide was isolated quantitatively by covalent affinity chromatography on Sepharose DTNB support of our own synthesis. The protein was prepared from the vital organs of rats exposed to heavy metals (Hg, Cd).Isolation of low-molecular weight polythiolate and thiolate proteins of a small number of SH-groups are reported. Changes in II and III order structure of the protein and aggregation resulting from chaotic formation of disulphide bridges were observed.A mechanism of separation of polythiolate proteins by covalent chromatography, based on the presented data, is suggested.Presented at the 17th International Symposium on Chromatography, September 25–30, 1988, Vienna, Austria.