[Two classes of lysine-binding sites of plasminogen molecule].
Affinity of plasminogen fragments K1, K2-3, K4 and K5 for 6-aminophenyl-Sepharose was investigated to characterize the lysine-binding sites of the protein. K1 and K5 fragments were bound to the affinity column, whereas kringle 2-3 and kringle 4 were not. The results obtained and data known from literature have indicate that two types of lysine-binding sites are present in the plasminogen molecule. Both positively and negatively charged groups of the ligand are necessary for binding with the first-type sites (K4 and K2-3). The interaction between ligands and the second-type sites localized in kringles 1 and 5 is provided by their positively charged group only.
Matsuka
Iu V
IuV
Novokhatniĭ
V V
VV
Kudinov
S A
SA
D001665:Binding Sites; D002846:Chromatography, Affinity; D006801:Humans; D007704:Kininogens / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation
D007704:Kininogens; D010446:Peptide Fragments; D008239:Lysine
Dva klassa lizinsviazyvaiushchikh uchastkov molekuly plazminogena.