Evaluation of the interaction of protein alpha-amino groups with M(II) by immobilized metal ion affinity chromatography.
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.
Andersson
L
L
Biochemical Separation Centre, University of Uppsala, Sweden.
Sulkowski
E
E
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
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