Factors influencing the separation of glu-plasminogen affinity forms I and II by affinity chromatography.
Native human plasminogen, the proenzyme of plasmin (E.C. 3.4.21.7) occurs in blood in two well defined forms, affinity forms I and II. In this paper, the feasibility of separating these forms of human native plasminogen by affinity chromatography, is shown to be dependent on two factors: 1) the ionic composition of the buffer containing the displacing agent: buffers of varying contents of sodium, Tris, phosphate and chloride ions were compared, and 2) the type of adsorbent. Two adsorbents were compared: Sepharose-lysine and Sepharose-bisoxirane-lysine. Only in the phosphate containing buffers, irrespective of the type of adsorbent, the affinity forms can be separated. The influence of the adsorbent can be accounted for by a large difference in dissociation constants of the complex between plasminogen and the immobilized lysine.
D000345:Affinity Labels; D002021:Buffers; D002846:Chromatography, Affinity; D006801:Humans; D009994:Osmolar Concentration; D010958:Plasminogen / Q000302:isolation & purification*; D012685:Sepharose / Q000031:analogs & derivatives
D000345:Affinity Labels; D002021:Buffers; C030675:lysine-sepharose; D010958:Plasminogen; D012685:Sepharose