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Identification of the binding site for plasminogen kringle 5 in the α-chain of fibrin(ogen) D-fragment

机译:纤溶酶原Kringle 5在纤维蛋白(ELIGON)D-碎片中的粒子原Kringle 5的鉴定

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The interaction of the fifth kringle of Glu-plasminogen with fibrin triggers activation and initiation of fibrinolysis, yet the site on fibrin that binds kringle 5 remains unknown. The aim of our work was to determine an amino acid sequence in the D-fragment of fibrin(ogen) molecule, which is complementary to the lysine-binding site (LBS) in kringle 5. We studied the interaction between kringle 5 of plasminogen with polypeptide chains of the D-fragments of fibrin and cyanogen bromide fragments FCB-2 and t-NDSK and showed that kringle 5 bound specifically to α- and γ-chains of the D-fragment and the α-chain of FCB-2. Tryptic peptides of D-fragment α-chain were obtained, separated by their ability to bind with the immobilized kringle 5, and then all studied peptides were characterized by MALDI-TOF analysis. The critical amino acid residues of the α-chain of D-fragment, which provide its interaction with kringle 5, turned out to be α171Arg and/or α176Lys. The binding site of Glu-plasminogen complementary to the LBS of kringle 5 is located within Аα168Ala?183Lys, a sequence in a weakly structured loop between two supercoils in the α-chain of the D-fragment of the fibrin(ogen) molecule.
机译:胶纤溶蛋白的第五kringle与纤维蛋白的相互作用触发纤维蛋白的激活和引发,然而纤维蛋白的位点仍然未知。我们的作品的目的是确定纤维蛋白(ELIGON)分子的D-片段中的氨基酸序列,其与Kringle 5中的赖氨酸结合位点(LBS)互补。我们研究了纤溶酶原的Kringle 5之间的相互作用纤维蛋白和氰基溴化物片段FCB-2和T-NDSK的多肽链和氰基碎片的碎片链条,并显示Kringle 5特异性地结合到D-片段的α-和γ-链和Fcb-2的α-链。获得D-碎片α链的胰蛋白酶肽,通过它们与固定的Kringle 5结合的能力分离,然后通过MALDI-TOF分析表征所有研究的肽。 D-片段的α链的临界氨基酸残基,其与Kringle 5提供其相互作用,结果为α171ARG和/或α176。与Kringle 5的LBS互补的Glu - 纤溶酶原的结合位点位于α168Alaα183ly内,在纤维蛋白(ELIGOL)分子的D-片段的D-片段的α链中的两种超级油之间的弱结构环中。

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