Biopolym. Cell. 1996; 12(5):38-45.
The role of regulatory arginyl-binding site of plasmine catalytic chain in fibrinogen hydrolysis
- Palladin Institute of Biochemistry, NAS of Ukraine
9, Leontovycha Str., Kyiv, Ukraine, 01601
Abstract
The effect of arginine and fibrinogen Dh-fragment on fibrinogenolysis velocity under the action of Lys77-plasmine and its partially degraded forms was studied. The results obtained revealed the low affinity to arginine of so-called arginyl-binding sites of the catalytic chain compared with arginyl-binding sites of the enzyme non-catalytic chain. At the same time fibrinogen hydrolysis inhibition at Dh-fragment presence was shown to be determined by the site located in the catalytic chain of Lys77- or Lys530-plasmine. This effect was found to occur at the stage of both X-fragments formation and their destruction. The role of catalytic chain regulatory site at some stages of fibrinogenolysis is discussed.
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References
[1]
Markus G, DePasquale JL, Wissler FC. Quantitative determination of the binding of epsilon-aminocaproic acid to native plasminogen. J Biol Chem. 1978;253(3):727-32.
[2]
Holleman WH, Andres WW, Weiss LJ. The relationship between the lysine and the p-aminobenzamidine binding sites on human plasminogen. Thromb Res. 1975;7(5):683-93.
[3]
Matsuka YuV. "The structure and localization of Plasminogen's Lysine Binding Sites (LBS)": Author. diss ... kand biol nauk. Kiev, 1989; 17 p.
[4]
Verevka SV, Kudinov SA, Grinenko TV. Arginyl-binding sites of human plasminogen. Doklady Akad Nauk Ukr SSR. Ser B. 1985; (1):56-9.
[5]
V?radi A, Patthy L. Kringle 5 of human plasminogen carries a benzamidine-binding site. Biochem Biophys Res Commun. 1981;103(1):97-102.
[6]
Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science. 1970;170(3962):1095-6.
[7]
Robbins KC, Summaria L. [10] Human plasminogen and plasmin. Methods Enzymol. 1970;184–99.
[8]
Powell JR, Castellino FJ. Isolation of human Val354 -plasminogen as an elastolytic fragment of human Glu1 -plasminogen. Biochem Biophys Res Commun. 1981;102(1):46-52.
[9]
Wu HL, Shi GY, Wohl RC, Bender ML. Structure and formation of microplasmin. Proc Natl Acad Sci U S A. 1987;84(24):8793-5.
[10]
Varetskaya TV. Microheterogenity of fibrinogen. Cryofibrinogen. Ukr Biokhim Zh. 1960; 32(1):13-24.
[11]
McConahey PJ, Dixon FJ. Radioiodination of proteins by the use of the chloramine-T method. Methods Enzymol. 1980;70(A):210-3.
[12]
Medved' LV, Novokhatny? VV, Privalov PL. Isolation and investigation of structural organization of active and inactive forms of fibrinogen D-fragment molecule. Mol Biol (Mosk). 1982;16(6):1195-202.
[13]
Lezhen TI, Kudinov SA. Effect of fragments E and D on the plasmin hydrolysis of the fibrin clot. Biokhimiia. 1986;51(6):967-9.
[14]
Rozenfel'd MA, Fateeva LA, Gontar' ID. Fibrinogen fragment D - inhibitor of fibrinolytic processes. Biokhimiia. 1983;48(7):1135-40.
[15]
Grinenko TV, Tret'iachenko VG, Kudinov SA, Medved' LV. Plasminogen-binding centers of molecules of fibrinogen, fibrin and products of their proteolysis. Biokhimiia. 1987;52(10):1732-9.
[16]
Kudinov SA, Lezhen TI. Interaction of plazminogen, plazmin heavy and light chains with fibrinogen D- and E-fragments. Doklady Akad Nauk Ukr SSR. Ser B. 1982; (6):61-3.
[17]
Zolotareva EN, Grinenko TV, Skomorovskaia EV, Kudinov SA. Effect of chemical modification of arginine residues of fibrinogen and its DH-fragment on the rate of hydrolysis of these proteins by plasminogen. Ukr Biokhim Zh. 1994;66(2):79-85.
[19]
Gorkun OV, Medved LV. Structural organization of early fibrinogen degradation products, X1 and X2-fragments produced by plasmin. Doklady Akad Nauk Ukr SSR. Ser B. 1984;(3):57-61.
[20]
Zolotariova EN. Estimaton the role of plasmin lysib- and argininl sites on separate stages of fibrinolen hydrolysis. Author Thesis kand biol nauk. Kyiv, 1995. 14p.
[21]
Zolotareva EN. Studding of role site plasmin for relation with lysine and arginine on early stages fibrin(ogen) hydrolysis. Biopolym Cell. 1995; 11(3-4):96-103.