Effect of Ultrasound on Structure and Functional Properties of Antithrombin III and Proteins of PPSB Complex

V. M. Shkumatov^1*, I. E. Adzerikho², J. A. Lesnikovich¹, and E. A. Cherniavsky¹

¹Research Institute of Physical Chemical Problems, Belarusian State University, ul. Leningradskaya 14, Minsk 220050, Belarus; fax: (375-17) 209-5461; E-mail: biopharm@bsu.by

²Department of Cardiology, Belarusian Medical Academy of Postgraduate Education, ul. P. Brovki 3, Minsk 220714, Belarus; fax: (375-17) 232-2533; E-mail: chekan@srpmi.minsk.by

^* To whom correspondence should be addressed.

Received February 21, 2003; Revision received June 30, 2003

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A combination of gel-permeation HPLC, affinity chromatography on heparin-Sepharose, gel electrophoresis, and estimation of inhibitory activity showed that effect of low-frequency ultrasound (26 W/cm², 37°C, pH 7.4) on homogeneous antithrombin III was accompanied by formation of aggregates and a latent form of serpin. Heparin and pentosan polysulfate stabilized antithrombin III; this resulted in decrease in ultrasonic-induced formation of the aggregate and latent forms. The influence of ultrasound was not accompanied by significant changes in the contents of non-activated blood coagulation factors in the PPSB complex.

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KEY WORDS: antithrombin III, latent and aggregate forms, ultrasound, PPSB complex

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