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Polydisulfides of Substituted Phenols as Effective Protectors of Peroxidase against Inactivation by Ultrasonic Cavitation

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Abstract

Kinetics of inactivation of horseradish peroxidase (HP) induced by low-frequency ultrasonic (US) treatment (27 kHz) with the specific power of 60 W/cm2 were studied in phosphate (pH 7.4) and acetate (pH 5.2) buffers within the temperature range of 36.0 to 50.0°C and characterized by effective first-order rate constants of US inactivation k in (us) in min−1. Values of k in (us) depend on the specific ultrasonic power within the range of 20-60 W/cm2, on the concentration of HP, and on pH and temperature of the solutions. The activation energy of US inactivation of HP is 9.4 kcal/mole. Scavengers of HO· radicals, mannitol and dimethylformamide, significantly inhibit the US inactivation of HP at 36.0°C, whereas micromolar concentrations of polydisulfide of gallic acid (poly(DSG)) and of poly(2-aminodisulfide-4-nitrophenol) (poly(ADSNP)) virtually completely suppress the US inactivation of peroxidase at the ultrasonic power of 60 W/cm2 on the sonication of the enzyme solutions for more than 1 h at pH 5.2. Various complexes of poly(DSG) with human serum albumin effectively protect HP against the US inactivation in phosphate buffer (pH 7.4). The findings unambiguously confirm a free radical mechanism of the US inactivation of HP in aqueous solutions. Polydisulfides of substituted phenols are very effective protectors of peroxidase against inactivation caused by US cavitation.

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Authors and Affiliations

  1. Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, ul. Kuprevicha 5/2, Minsk, 220141, Belarus

    E. E. Grintsevich & D. I. Metelitza

  2. Belorussian State Institute of Physician Improvement, ul. P. Brovki 3, Minsk, 220714, Belarus

    I. E. Adzerikho & A. G. Mrochek

Authors
  1. E. E. Grintsevich
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  2. I. E. Adzerikho
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  3. A. G. Mrochek
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  4. D. I. Metelitza
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Grintsevich, E.E., Adzerikho, I.E., Mrochek, A.G. et al. Polydisulfides of Substituted Phenols as Effective Protectors of Peroxidase against Inactivation by Ultrasonic Cavitation. Biochemistry (Moscow) 66, 740–746 (2001). https://doi.org/10.1023/A:1010256511200

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