Neutralization anticoagulant activity of sulfates of the cellulose excreted from Gossypium hirsutum L. by protamine sulfate

A.A. Kuzhim; N.N. Drozd; M.A. Torlopov

Neutralization anticoagulant activity of sulfates of the cellulose excreted from Gossypium hirsutum L. by protamine sulfate

A.A. Kuzhim¹, N.N. Drozd², M.A. Torlopov³

research article Pages: 34-38

¹ Post-graduate Student, Hematology Research Center, Moscow, Russia
² Dr.Sc. (Biol.), Leading Research Scientist, Hematology Research Center, Moscow, Russia
³ Ph.D. (Chem.), Research Scientist, Institute of Chemistry Komi Science Center Ural Branch of the Russian Academy of Sciences, Syktyvkar, Russia

Keywords: cellulose sulfate protamine sulfate anticoagulant / antithrombin activity neutralization anticoagulant/anti-thrombin activity

Abstract

It was investigated anticoagulant activity of sulfates of the cellulose excreted from Gossypium hirsutum L. Cellulose sulfates increase plasma coagulation time of appearance of human plasma fibrin clots in coagulation tests - activated particulate thromboplastin time, prothrombin time, thrombin time and ReaClot-Heparin.

How to cite

Кужим А.А., Дрозд Н.Н., Торлопов М.А. Нейтрализация сульфатом протамина антикоагулянтной активности сульфатированной целлюлозы, выделенной из Gossypium hirsutum L // Вопросы биологической, медицинской и фармацевтической химии. 2014. № 1. С. 34–38.

References

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Jiao G., Yu G., Zhang J. et al. Chemical Structures and Bioactivities of Sulfated Polysaccharides from Marine Algae // Mar. Drugs.2011. V. 9. № 2. P. 196-223.
Pai M., Crowther M. Neutralization of heparin activity // Handb. Exp. Pharmacol. 2012. № 207. P. 265-277.
Torlopov M.A. Sul'fatirovanie mikrokristallicheskoj czellyulozy' s ispol'zovaniem ul'trazvukovoj aktivaczii v srede N,N-dimetilformamida // Ximiya v interesax ustojchivogo razvitiya. 2011. T. 19. № 5. S. 555-559.
Funk D.M. Coagulation assays and anticoagulant monitoring // Hematology Am. Soc. Hematol. Educ. Program. 2012. V. 2012. P. 460-465.
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Teien A., Lie M., Abildgaard U. Assay of heparin in plasma using a chromogenic substrate for activated factor X // Thromb. Res.1976. V. 8. № 3. P. 413-416.
de Araújo C., Noseda M., Cipriani T. et al. Selective sulfation of carrageenans and the influence of sulfate regiochemistry on anticoagulant properties // Carbohydr. Polym. 2013. V. 91. № 2. P. 483-491.
Farias W., Valente A., Pereira M., et al. Structure and anticoagulant activity of sulfated galactans // J. Biol. Chem. 2000. V. 275. № 38. P. 29299-29307.
Wang Z., Li L., Xiao K. et al. Homogeneous sulfation of bagasse cellulose in an ionic liquid and anticoagulation activity // Bioresour. Technol. 2009. V. 100. № 4. P. 1687-1690.
Chawla L., Moore G., Seneff M. Incomplete reversal of enoxaparin toxicity by protamine: implications of renal insufficiency, obesity, and low molecular weight heparin sulfate content // Obes. Surg. 2004. V. 14. № 5. P. 695-698.
Maurer J., Haselbach S., Klein O. et al. Analysis of the complex formation of heparin with protamine by light scattering and analytical ultracentrifugation: implications for blood coagulation management // J. Am. Chem. Soc. 2011. V. 133. № 4. P. 1134-1140.
Cumming A., Jones G., Wensley R. et al. In vitro neutralization of heparin in plasma prior to the activated partial thromboplastin time test: an assessment of four heparin antagonists and two anion exchange resins // Thromb. Res. 1986. V. 41. № 1. P.43-56.
Young E., Cosmi B., Weitz J. et al. Comparison of the non-specific binding of unfractionated heparin and low molecular weight heparin (Enoxaparin) to plasma proteins // Thromb. Haemost. 1993. V. 70. № 4. P. 625 - 630.
Ramamurthy N., Baliga N., Wakefield T. et al. Determination of low-molecular-weight heparins and their binding to protamine and a protamine analog using polyion-sensitive membrane electrodes // Analytical Biochemistry. 1999. V. 266. № 1. P. 116-124.
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[1] Bhaskar U., Sterner E., Hickey A. et al. Engineering of routes to heparin and related polysaccharides // Appl. Microbiol. Biotechnol. 2012. V. 93. № 1. P. 1-16.

[2] Jiao G., Yu G., Zhang J. et al. Chemical Structures and Bioactivities of Sulfated Polysaccharides from Marine Algae // Mar. Drugs.2011. V. 9. № 2. P. 196-223.

[3] Pai M., Crowther M. Neutralization of heparin activity // Handb. Exp. Pharmacol. 2012. № 207. P. 265-277.

[4] Torlopov M.A. Sul'fatirovanie mikrokristallicheskoj czellyulozy' s ispol'zovaniem ul'trazvukovoj aktivaczii v srede N,N-dimetilformamida // Ximiya v interesax ustojchivogo razvitiya. 2011. T. 19. № 5. S. 555-559.

[5] Funk D.M. Coagulation assays and anticoagulant monitoring // Hematology Am. Soc. Hematol. Educ. Program. 2012. V. 2012. P. 460-465.

[6] Teien A., Lie M. Evaluation of an amidolytic heparin assay method: increased sensitivity by adding purified antithrombin III // Thromb. Res. 1977. V. 10. № 3. P. 399-410.

[7] Teien A., Lie M., Abildgaard U. Assay of heparin in plasma using a chromogenic substrate for activated factor X // Thromb. Res.1976. V. 8. № 3. P. 413-416.

[8] de Araújo C., Noseda M., Cipriani T. et al. Selective sulfation of carrageenans and the influence of sulfate regiochemistry on anticoagulant properties // Carbohydr. Polym. 2013. V. 91. № 2. P. 483-491.

[9] Farias W., Valente A., Pereira M., et al. Structure and anticoagulant activity of sulfated galactans // J. Biol. Chem. 2000. V. 275. № 38. P. 29299-29307.

[10] Wang Z., Li L., Xiao K. et al. Homogeneous sulfation of bagasse cellulose in an ionic liquid and anticoagulation activity // Bioresour. Technol. 2009. V. 100. № 4. P. 1687-1690.

[11] Chawla L., Moore G., Seneff M. Incomplete reversal of enoxaparin toxicity by protamine: implications of renal insufficiency, obesity, and low molecular weight heparin sulfate content // Obes. Surg. 2004. V. 14. № 5. P. 695-698.

[12] Maurer J., Haselbach S., Klein O. et al. Analysis of the complex formation of heparin with protamine by light scattering and analytical ultracentrifugation: implications for blood coagulation management // J. Am. Chem. Soc. 2011. V. 133. № 4. P. 1134-1140.

[13] Cumming A., Jones G., Wensley R. et al. In vitro neutralization of heparin in plasma prior to the activated partial thromboplastin time test: an assessment of four heparin antagonists and two anion exchange resins // Thromb. Res. 1986. V. 41. № 1. P.43-56.

[14] Young E., Cosmi B., Weitz J. et al. Comparison of the non-specific binding of unfractionated heparin and low molecular weight heparin (Enoxaparin) to plasma proteins // Thromb. Haemost. 1993. V. 70. № 4. P. 625 - 630.

[15] Ramamurthy N., Baliga N., Wakefield T. et al. Determination of low-molecular-weight heparins and their binding to protamine and a protamine analog using polyion-sensitive membrane electrodes // Analytical Biochemistry. 1999. V. 266. № 1. P. 116-124.

[16] Okano K., Saito Y., Matsushima A. et al. Protamine interacts with the D-domains of fibrinogen // Biochim. Biophys. Acta. 1981. V. 671. № 2. P. 164-167.