Studding of role site plasmin for relation with lysine and arginine on early stages fibrin(ogen) hydrolysis

Authors

  • E. N. Zolotareva Palladin Institute of Biochemistry, NAS of Ukraine 9, Leontovycha Str., Kyiv, Ukraine, 01601 Author

DOI:

https://doi.org/10.7124/bc.0003F2

Abstract

The effect of 6-aminohexane acid (6-AHA) and L-arginine on the rates of early stages of fibrinogen hydrolysis by Lys77-plasmin, Val442-plasmin and Lys530-plasmin were studded. It was shown that 6-AHA on the second reaction stage (hydrolysis of X) in the concentrations saturating the site, of plasmin heavy chain had a strong inhibiting influence even more stronger than a the first stage (hydrolysis of fibrinogen). Effect of arginine and 6-AHA on the first stage hydrolysis was identical. Arginine effect on the second stage failed to be observed while its concentration were effecting kringle 1 and 5. It was suggested the enzyme interaction with substrate took place on the first stage of hydrolysis under kringles 5 and 1 patrkipation on second stage – under kringle 4 participation.

References

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.

Trexler M, Váli Z, Patthy L. Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4. J Biol Chem. 1982;257(13):7401-6.

Winn ES, Hu SP, Hochschwender SM, Laursen RA. Studies on the lysine-binding sites of human plasminogen. The effect of ligand structure on the binding of lysine analogs to plasminogen. Eur J Biochem. 1980;104(2):579-86.

Verevka SV, Kudinov SA, Grinenko TV. Arginyl-binding sites of human plasminogen. Thromb Res. 1986;41(5):689-98.

Matsuka YuV. Localization and structural characterization of lysine-binding sites of plasminogen molecule: Author. Dis .... kand. biol. Sciences. Kiev, 1989; 17 p.

Ney KA, Pizzo SV. Fibrinolysis and fibrinogenolysis by Val442-plasmin. Biochim Biophys Acta. 1982;708(2):218-24.

Morris JP, Castellino FJ. The role of the lysine binding sites of human plasmin in the hydrolysis of human fibrinogen. Biochim Biophys Acta. 1983;744(1):99-104.

Andrianov SI, Makogonenko EM, Kudinov SA. Role of the K4 and K5 plasmin heavy chain kringles in the fibrin clot structure destruction. Ukr Biokhim Zh. 1992;64(2):31-8.

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.

Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science. 1970;170(3962):1095-6.

Robbins KC, Summaria L. Human plasminogen and plasmin. Methods Enzymol.1970;184–99.

Varetska TV. Microheterogeneity of fibrinogen. Cryofibrinogen. Ukr Biokhim Zh. 1960; 32(1):13-24.

McConahey PJ, Dixon FJ. Radioiodination of proteins by the use of the chloramine-T method. Methods Enzymol. 1980;70(A):210-3.

Medved LV, Gorkun OV, Privalov PL. Structural organization of C-terminal parts of fibrinogen A alpha-chains. FEBS Lett. 1983;160(1-2):291-5.

Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971;10(13):2606-17.

Matsuka IuV, Novokhatniĭ VV, Kudinov SA. Two classes of lysine-binding sites of plasminogen molecule. Ukr Biokhim Zh. 1990;62(2):83-6.

Samson E, Chrisflan Petersen L. Exact temporal correlation of the rapid phase of t-PA catalyzed plasminogen (LPG) activation during fibrinolysis, with PLG binding to the D-D-E domains of fragment x polymers. Fibrinolysis. 1989;3:17.

Svenson E, Koek T, Petersen LC. Functional binding of plasminogen to fibrin fragment X-polymer-involves simultaneous binding of high-affinity and kringle 5 lysine-binding sites. Fibrinolysis. 1990; 4( 3): 99.

Published

1995-07-20

Issue

Section

Biopolymers and Cell