Arginyl-binding sites of human plasminogen.
Localization and specific features of lysine- and arginyl-binding sites in Lys-plasminogen, its fragments and domains have been investigated by affinity chromatography on the sorbents containing arginine-like ligands. Lysine-binding sites of Lys-plasminogen, heavy chain and fragment K1-3 interact with the guanidyl-carboxyl pair on homoarginine-agarose. Lysine-binding site in domain K4, interacting with the amine-carboxyl pair on lysine-agarose, does not interact with that of guanidyl-carboxyl. It has been found that plasminogen contained three arginyl-binding sites interacting with guanidyl group in homoarginine-agarose. Two of them correspond to two benzamidine-binding sites in domain K5 and to the plasmin light chain while the third (unknown before) is located in fragment K1-3 and does not interact with benzamidine-agarose.
S V
SV
Verevka
S A
SA
Kudinov
T V
TV
Grinenko
D001120:Arginine / Q000378:metabolism*; D001550:Benzamidines / Q000378:metabolism; D001665:Binding Sites; D002846:Chromatography, Affinity; D006709:Homoarginine / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008239:Lysine / Q000378:metabolism; D010958:Plasminogen / Q000032:analysis*
D001550:Benzamidines; D008024:Ligands; D006709:Homoarginine; D010958:Plasminogen; D001120:Arginine; D008239:Lysine; C032157:benzamidine