Affinity chromatography on hydroxyalkyl methacrylate gels. II. Isolation of thiol-containing protein and peptide using mercurial derivatives of gels.

Absorption properties of hydroxyalkyl methacrylate gels containing various amounts of mercuri derivatives of p-acetaminophenoxyethyl methacrylates (Hg-APEMA) and methacrylanilide (Hg-MAA) were investigated by means of a reduced Ellman's agent (5,5'-dithiobis-2-nitrobenzoic acid) and papain. The optimum gel was used for the affinity chromatography of SH-protease from beans and for the isolation of a peptide with a free sulphhydryl group from the chymotryptic hydrolyzate of serum albumin.