L. G. Kapustianenko, T. Grinenko, A. Rebriev, O. Yusova, A. Tykhomyrov
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引用次数: 0
Abstract
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 αand 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 Dfragment of the fibrin(ogen) molecule.
期刊介绍:
The Ukrainian Biochemical Journal publishes original research papers, reviews and brief notes; papers on research methods and techniques; articles on the history of biochemistry, its development and prominent figures; discussion articles; book reviews; chronicles; etc. The journal scope includes not only biochemistry but also related sciences, such as cellular and molecular biology, bioorganic chemistry, biophysics, pharmacology, genetics, and medicine (medical biochemistry et al.) – insofar as the studies use biochemical methods and discuss biochemical findings.