ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)
Biotechnologia Acta V. 15, No. 3, 2022
P. 23-28, Bibliography 18, Engl.
UDC: 577.112:612.115
https://doi.org/10.15407/biotech15.03.023
Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine
Aim. Study of the role of the complex between the αC region and the BβN domain in the initial stages of fibrin polymerization has been investigated.
Materials and Methods. Method of turbidimetry to study the influence of fibrinogen fragments D and DD on the polymerization and methods of isolation, purification, fragmentation for fibrinogen, monomer and cross-linked fibrin, fibrinogen X-fragment, Glu -plasminogen were used.
Results. It was shown that fragment DD completely inhibited polymerization process in all the systems examined (“Fg + Thr”, “Fg + Anc H”, “X + Thr”, “X + Anc H”). Fragment D inhibited fibrin polymerization at all stages in the system “Fg + Thr”, but in the system “Fg + Anc H” it almost did not influence fibrin polymerization. In the both systems “X + Thr” and “X + Anc H” fragment D weakly inhibited the self-assembly of fibrin molecules into protofibrils, but accelerated the process of lateral association in the second system.
Conclusions. The data obtained indicated that the complex between the αC region and the BβN domain of fibrin desA, on the initial stage of polymerization supported the rate of self-assembling and lateral association of fibrin desA protofibrils, protecting the oligomers against the depolymerizing influence of fibrinogen.
Key words: fibrinogen, fibrin, fragment DD, D dimer, fragment X, BβN-domain-αC-region complex.
© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2022
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