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.
D002021:Buffers; D002846:Chromatography, Affinity; D002918:Chymotrypsin; D004228:Dithionitrobenzoic Acid; D006863:Hydrogen-Ion Concentration; D008628:Mercury; D008689:Methacrylates; D010206:Papain; D010446:Peptide Fragments / Q000302:isolation & purification*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D010944:Plants; D012709:Serum Albumin; D013438:Sulfhydryl Compounds / Q000302:isolation & purification*
D002021:Buffers; D008689:Methacrylates; D010446:Peptide Fragments; D012709:Serum Albumin; D013438:Sulfhydryl Compounds; D004228:Dithionitrobenzoic Acid; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D010206:Papain; D008628:Mercury