title: [Two classes of lysine-binding sites of plasminogen molecule].
abstract: 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.
authors.forename: Iu V
authors.initials: IuV
authors.lastname: Matsuka
authors.forename: V V
authors.initials: VV
authors.lastname: Novokhatniĭ
authors.forename: S A
authors.initials: SA
authors.lastname: Kudinov
mesh_terms: D001665:Binding Sites; D002846:Chromatography, Affinity; D006801:Humans; D007704:Kininogens / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D007704:Kininogens; D010446:Peptide Fragments; D008239:Lysine
vernacular_title: Dva klassa lizinsviazyvaiushchikh uchastkov molekuly plazminogena.