Biopolym. Cell. 2005; 21(1):28-34.
Structure and Function of Biopolymers
Rat liver catalase under artificial hypobiosis conditions
1Gudkova O. O., 1Latyshko N. V., 1Gudkova L. V., 1Mikhailovsky V. O.
  1. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601

Abstract

The peculiarities of antioxidant enzyme catalase action in hyber­nation were studied. In vivo and in vitro assays show that (HCO3 -CO2) activates rat liver catalase. It was determined that between pH 7.2 and 8.5 the enzyme was stable when the carbon concentration was constant. The catalase KM values at norm and hypobiosis are of the same level. Nevertheless, the enzyme kcat and kcat/KM values rise was established under the hypobiosis conditions. This increase relates to a greater biocatalyst efficiency rather than to a higher level of its synthesis.
Keywords: catalase, hypobiosis, carbon dioxide, polyamines

References

[1] Mel'nychuk DO, Mykha?lovsky? VO, Mel'nychuk SD. [Mechanism of metabolic adaptation]. Ukr Biokhim Zh. 2000;72(4-5):70-80.
[2] Kuzmenko AI, Mikhailovsky VO. Free-radical lipid oxidation at the deep hypothermid and amiles action. Int Congr «Stress and adaptation from molecules to man» (Budapest, 1—5 July 1997) Budapest, 1997; 86.
[3] Andjus RK, Smith AU. Reanimation of adult rats from body temperatures between 0 and + 2 degrees C. J Physiol. 1955;128(3):446-72.
[4] Mel'nychuk SD, Rohovs'ky? SP, Mel'nychuk DO. [Acid-base equilibrium and nitrogen metabolism in rats in a state of artificial hibernation]. Ukr Biokhim Zh. 1995;67(4):67-75.
[5] Ignat'ev DA, Kolaeva SG, Kramarova LI, Kravchenko II. [Hypothermic effect on mice of a 1-10 kD fraction of the small intestine of the hibernating suslik Citellus undulatus during hypoxia and hypercapnia]. Zh Evol Biokhim Fiziol. 1989;25(3):318-23.
[6] Timofeev NN. Artificial hibernation. M.: Meditsina, 1983. 192 p.
[7] Mikhailovsky VO. Features of regulation of ornithine decarboxylase under extreme conditions. Proceedings of the 5th All-union. Symposium med enzymology. Makhachkala, 1986:76.
[8] Samner OB. Chemistry of enzymes and methods of their research. M, 1948; 250 p.
[9] Lebedeva EI, Levina LSh. Determination of the activity of the enzyme catalase: Scientific and Technical Information. M.: CINTIPISEPROM, 1965; 4:6 p.
[10] SIGMA, Biochemicals and Reagents New York, 1999; 229 p.
[11] Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193(1):265-75.
[12] Filipovich YuB, Egorova TA, Sevast'yanova TA. Quantitative determination of the protein of the biuret reaction. Practicals on the general Biochemistry. M, 1982; 268 p.
[13] Price VE, Sterling WR, Tarantola VA, Hartley RW Jr, Rechcigl M Jr. The kinetics of catalase synthesis and destruction in vivo. J Biol Chem. 1962;237:3468-75.
[14] Koroliuk MA, Ivanova LI, Ma?orova IG, Tokarev VE. [A method of determining catalase activity]. Lab Delo. 1988;(1):16-9.
[15] Smirnov AV, Krivoruchko BI, Zarubina IV, Mironova OP. [Protective effects of trimetazidine during acute hypoxia]. Biull Eksp Biol Med. 1998;125(4):410-2.
[16] Mikhailovsky VO. Adaptive regulation of polyamine metabolism in animals under natural and artificial cooling. Tez. . 1st Congress Ukr Soc Cryobiology and Cryomedicine. Kharkiv, 1995;170-1.
[17] Latyshko NV, Gudkova LV. [The kinetic and catalytic properties of Penicillium vitale catalase]. Ukr Biokhim Zh. 1996;68(2):69-73.