Involvement of the lysine-binding sites of plasminogen on its interaction with concanavalin A.
Two different interactions are involved in the binding of plasminogen to concanavalin A-Sepharose: both variants 1 and 2 interact with the lectin through the lysine-binding sites and, in addition, variant 1 binds to concanavalin A due to carbohydrate recognition. Both kinds of interactions were also observed in solution by analytical ultracentrifugation. The binding of Lys-plasminogen to concanavalin A via lysine-binding sites largely exceeds that of Glu-plasminogen, in accordance with the higher affinity for lysine of Lys-plasminogen. This fact can be applied to the separation of both forms of plasminogen in a single chromatographic step.
Arias
M
M
Instituto de Química Física "Rocasolano", Madrid, Spain.
Solís
D
D
Díaz-Mauriño
T
T
D001665:Binding Sites; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008239:Lysine / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism; D010958:Plasminogen / Q000302:isolation & purification / Q000378:metabolism*; D012685:Sepharose / Q000031:analogs & derivatives
D010446:Peptide Fragments; C028326:concanavalin A-sepharose; C018998:lysyl-plasminogen; D003208:Concanavalin A; D010958:Plasminogen; D012685:Sepharose; D008239:Lysine