The obtaining of succinate dehydrogenase from flight muscles of bumble bees Bombus terrestris using ion-exchange chromotography

  • Tatyana M. Gorbacheva graduate student, Department of biochemistry and physiology, Voronezh State University, Voronezh, E-mail: sokitanya@ yandex.ru
  • Mihail Yu. Syromyatnikov master of biology, Department of biochemistry and physiology, Voronezh State University, Voronezh
  • Vasilij N. Popov doctor of biology, professor, Department of biochemistry and physiology, Voronezh State University, Voronezh
  • Aleksej V. Lopatin candidate of biology, Department of entomology, Voronezh State University, Voronezh
Keywords: succinate dehydrogenase (SDH), ion-exchange chromatography, isofom, bumble bee, Bombus terrestris.

Abstract

An effective procedure for purification of the succinate dehydrogenase from mitochondria of
flight muscles of bumble bee Bombus terrestris has been developed. The procedure includes fractionation
of proteins from the mitochondrial fraction by ammonium sulfate, gel filtration, ion-exchange
chromatography on DEAE-cellulose. The enzyme was purified up to homogeneity. The specific activity
of homogeneous preparation was 7.14 units per mg of protein. The enzyme from flight muscles of bumble
bee is made up of one isoform. The substrate specificity has been investigated

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References

1. Виноградов А.Д. Сукцинат-убихинон редуктазный участок дыхательной цепи /
А.Д. Виноградов // Биохимия. − 1986. − Т. 51. − №12. − С. 1944-1973.
2. Singer T.P. Solubilisation assay and purification of succinate dehydrogenase / T.P.
Singer, E.B. Rsarney // Biochem et Biophys. Akta. − 1954. − Vol. 15. − P. 151-153.
3. Cooper T.G. Mitochondria and glyoxysomes from castor bean endosperm. enzyme
constitutents and catalytic capacity / T.G. Cooper, H.J. Beevers // J.Biol. Chem. - 1969. -
Vol. 244. - P. 3507–3513.
4. Protein measurement with the Folin phenol reagent / O.H. Lowry [et al.] // J. Biol.
Chem. –1951. – vol. 193. - №1. – pp. 265-275.
5. Davis B.J. Disc electrophoresis II. Method and aplication to human serum protein /
B.J. Davis // Ann. N. Y. Acad. Sci. - 1994. – Vol. 121. – P. 404-427.
6. Shevchenko A., Wilm M., Vorm O. Mass spectrometric sequncing of protein from
silver-stained polyarylamide gels // Anal. Chem., 1996. V.68. P. 850-858.
7. Гааль, Э., Медьеши Г., Верецкий Л. Электрофорез в разделении биологических
макромолекул. М.: Мир, 1982. 446 с.
8. Ackrell A.C. Effect of membrane environment on succinate dehydrogenase activity /
A.C. Ackrell, E.B. Kearney // The Journal of Biological Chemistry. – 1976 – Vol. 252. -
№5. – P. 1582-1588.
9. Manadori A. (3Fe-4S) to (4Fe-4S) cluster conversion in Escherihia coli fumarate
reductase by site directed mutagenesis / A. Manodori, G. Cecchini, M. K. Jonson //
Biochemistry. – 1992.- Vol.31 - №10. – P. 2703-2712.
10. Holingren E., Hederstedt L. Rufberg L. // J.Bacteriol. 1979. V.138. N 2. P.377-382
11. Hattori T., Asahi T. // Plant and Cell Physiol. 1982. V.23. N 2. P.515-523.
12. Insect biochemistry and function / edited by D. J. Candy and B. A. Kilby 1936
Published
2019-11-26
How to Cite
Gorbacheva, T. M., Syromyatnikov, M. Y., Popov, V. N., & Lopatin, A. V. (2019). The obtaining of succinate dehydrogenase from flight muscles of bumble bees Bombus terrestris using ion-exchange chromotography. Sorbtsionnye I Khromatograficheskie Protsessy, 11(5). Retrieved from https://journals.vsu.ru/sorpchrom/article/view/1973