Factors influencing the separation of Glu-plasminogen affinity forms I and II by affinity chromatography

article
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. Chemicals/CAS: plasminogen, 9001-91-6; Affinity Labels; Buffers; lysine-sepharose; Plasminogen, 9001-91-6; Sepharose, 9012-36-6
TNO Identifier
229721
ISSN
0340-6245
Source
Thrombosis and Haemostasis, 52(3), pp. 347-349.
Pages
347-349
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