Two classes of lysine-binding sites of plasminogen molecule
Matsuka, I.V.; Novokhatniĭ, V.V.; Kudinov, S.A.
Ukrainskii Biokhimicheskii Zhurnal 62(2): 83-86
1990
ISSN/ISBN: 0201-8470 PMID: 2114684 Document Number: 363797
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 I and 5 is provided by their positively charged group only.