title: Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.
abstract: The adsorption properties of various peptides and proteins, lacking histidyl groups, on immobilized Cu(II), Ni(II), Zn(II) and Co(II) ions are described; at pH 6 and below they were little retarded. At higher pH the retention became pronounced for iminodiacetate (IDA)-Cu(II) gel. This effect seems to be related to the presence of a terminal alpha-amino group; in the absence of this group the retention of the protein was largely eliminated. At pH 8.5 a terminal alpha-amino group is adsorbed as strongly as a histidyl group. IDA-Ni(II), IDA-Zn(II) and IDA-Co(II) gels display little or no attraction for the terminal alpha-amino group of a protein.
authors.affiliation: Biochemical Separation Centre, University of Uppsala, Sweden.
authors.forename: L
authors.initials: L
authors.lastname: Andersson
authors.forename: E
authors.initials: E
authors.lastname: Sulkowski
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000737:chemistry; D002413:Cations, Divalent; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods*; D003300:Copper / Q000737:chemistry; D004372:Ducks; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000737:chemistry*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry; D009532:Nickel / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013549:Sweetening Agents; D015032:Zinc / Q000737:chemistry
chemical_list: D002413:Cations, Divalent; D008670:Metals; D010940:Plant Proteins; D011506:Proteins; D013549:Sweetening Agents; C003427:thaumatin protein, plant; D003300:Copper; D009532:Nickel; D007611:Aprotinin; D009113:Muramidase; D015032:Zinc