Matsuka Iu V, Novokhatniĭ V V, Kudinov S A
Ukr Biokhim Zh (1978). 1990 Mar-Apr;62(2):83-6.
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.
研究了纤溶酶原片段K1、K2 - 3、K4和K5对6 - 氨基苯基 - 琼脂糖的亲和力，以表征该蛋白的赖氨酸结合位点。K1和K5片段与亲和柱结合，而kringle 2 - 3和kringle 4则不结合。所得结果及文献已知数据表明，纤溶酶原分子中存在两种类型的赖氨酸结合位点。配体的带正电和带负电基团对于与第一类位点（K4和K2 - 3）结合都是必需的。配体与位于kringles 1和5中的第二类位点之间的相互作用仅由其带正电基团提供。
