Using chromatographic methods for the purification of the key enzymes of the glyoxylate cycle from organisms of different taxonomic groups
Keywords:
glyoxylate cycle enzyme, gel chromatography, ion-exchange chromatography purification.
Abstract
The article presents an overview of methods for the isolation of key enzymes of the glyoxylate cycle
of organisms from different taxonomic groups using gel chromatography and ion exchange chromatography.
The main interest of the study of the functioning of the glyoxylate cycle enzyme is the study of isocitrate
lyase (ICL), akoninate hydratase (AH) and malate dehydrogenase (MDH). At the first stage, gel filtration
with Sephadex in order to relief from low molecular weight particles is used most often, then goes driven
ion-exchange chromatography on DEAE-cellulose or DEAE-Toyopearl. The final step is using gel column
chromatography with large pore sizes. The process of glyoxylate cycle enzymes purification from organisms
of different taxonomic groups was developed at the Department of Biochemistry and Cell Physiology of
Voronezh State University. This purification scheme allowed us to receive glyoxylate cycle enzymes
preparations (MDH, ICL, AH) with high specific activity
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References
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V.N. Induction of aconitate hydratase in
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No 4, pp. 376-80.
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M.T., Fernandez R., Moreno F. Purification of
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Purification and characterization of isocitrate
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pp. 258-260.
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A.T., Igamberdiev A.U. Induction of glyoxylate
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rats, Izv. Akad Nauk Ser. Biol, 2000, V. 6, pp.
672-678.
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A.T., Igamberdiev A.U. Glyoxylate cycle
enzymes are present in liver peroxisomes of
alloxan-treated rats, FEBS Lett, 1998, V. 440,
No 1-2, pp. 55-58.
19. Popov V.N., Volvenkin S. V., Kosmatykh
T. A. et al. Induction of a peroxisomal malate
dehydrogenase isoform in liver of starved rats,
Biochemistry (Mosc), 2001, V. 66, No 5, pp.
496-501.
20. Ruchti M., Widmer F. Isocitrate lyase
from germinating soybean cotyledons:
purification and characterization, J. exp. Bot,
1986, V. 37, pp. 1685-1690.
21. Vincenzini M.T., Nerozzi F., Vincieri
F.F., Vanni P. Isolation and properties of
isocitrate lyase from Lupinus seed,
Phytochemistry, 1980, V. 19, No 5, pp. 769-
774.
22. Watanabe S., Yamaoka N., Fukunaga N.,
Takada Y. Purification and characterization of a
cold-adapted isocitrate lyase and expression
analysis of the cold-inducible isocitrate lyase
gene from the psychrophilic bacterium
Colwellia psychrerythraea, Extremophiles,
2002, V. 6, No 5, pp. 397-405.
23. Dingman D.W., Sonenshein A.L.
Purification of aconitase from Bacillus subtilis
and correlation of its N-terminal amino acid
sequence with the sequence of the citB gene, J.
Bacteriol, 1987, V. 169, No 7, pp. 3062-3067.
cell constituents from C2-units by a modified
tricarboxylic acid cycle, Nature, 1957, V. 179,
pp. 988-991.
2. Eprintsev A.T., Popov V.N., Shevchenko
M.Yu. Glioksilatnyi tsikl: universal'nyi
mekhanizm adaptatsii? [Glyoxylate cycle: a
universal mechanism for adaptation], Moskva.
IKTs «Akademkniga», 2007, 228 p.
3. Eprintsev A.T., Shevchenko M.Yu., Popov
V.N. Rasprostranenie glioksilatnogo tsikla u
organizmov razlichnykh taksonomicheskikh
grupp [Distribution of the glyoxylate cycle in
organisms of different taxonomic groups] //
Uspekhi sovremennoi biologii. M., 2008, V.
128, No 3, pp. 271-280.
4. Popov V.N. , Moskalev E.A., Shevchenko
M.Yu., Eprintsev A.T. Sravnitel'nyi analiz
klyuchevogo fermenta glioksilatnogo tsikla,
izotsitratliazy, iz organizmov raznykh
sistematicheskikh grupp [Comparative analysis
of the key enzyme of the glyoxylate cycle,
isocitrate lyase, from organisms of different
taxonomic groups], Zhurnal evolyutsionnoi
fiziologii i biokhimii, 2005, No 6, pp. 776-781.
5. Determan G. Gel'-khromatografiya [Gel
chromatography], M. Mir, 1970, 173 p.
6. De Lucasa J.R., Amora C., Díazla M.,
Turnerb G., Laborda F. Purification and
properties of isocitrate lyase from Aspergillus
nidulans, a model enzyme to study catabolite
inactivation in filamentous fungi, Mycological
Research, 1997, V. 101,. No 4, pp. 410-414.
7. Eprintsev A.T., Semenova E.V., Popov
V.N. Induction of aconitate hydratase in
hepatocytes of starving rats, Biochemistry
(Mosc), 2002, V. 67, No 7, pp. 795-801.
8. Eprintsev A.T., Shevchenko M.Y., Popov
V.N. Purification and properties of isocitrate
lyase from pupas of the butterfly Papilio
machaon L, Biochemistry (Mosc), 2004, V. 69,
No 4, pp. 376-80.
9. Hoyt J.C., Johnson K.E., Reeves H.C.
Purification and characterization of
Acinetobacter calcoaceticus isocitrate lyase, J
Bacteriol, 1991, V. 173, No 21, pp. 6844-6848.
10. John P.C., Syrett P.J. The purification and
properties of isocitrate lyase from Chlorella,
Biochem. J, 1967, V. 105, No 1, pp. 409-416.
11. Kamel M.Y., Fahmy A.S. Biochemical
studies of tick embriogenesis. Purification and
partial characterisation of isocitrate lyase from
eggs of the tick Hyalomma dromedarii,Comp.
Biochem. Physiol. B, 1982, V. 72, pp. 107-115.
12. Liu F., Thatcher J.D., Barral J.M.
Bifunctional glyoxylate cycle protein of
Caenorhabditis elegans: a developmentally
regulated protein of intestine and muscle, Dev.
Biol, 1995, V. 169, pp. 399-414.
13. Lopez-Boado Y.S., Herrero P., Fernandez
M.T., Fernandez R., Moreno F. Purification of
isocitrate lyase from Saccharomyces cerevisiae,
Yeast, 1988, V. 4, No 1,pp. 41-46.
14. Munir E., Hattori T., Shimada M.
Purification and characterization of isocitrate
lyase from the wood-destroying basidiomycete
Fomitopsis palustris grown on glucose, Arch.
Biochem. Biophys, 2002, V. 399, No 2, pp.
225-231.
15. Nakamura K., Amano Y., Nakadate M.,
Kagami M. Purification and properties of
isocitrate lyase from candida brassicae e 17. J.
of Fermentation & Bioengineering, 1989, V.
67, No 3, pp. 153-157.
16. Popov V.N., Igamberdiev A.U.,
Schnarrenberger C., Volvenkin S.V. Induction
of glyoxylate cycle enzymes in rat liver upon
food starvation, FEBS Lett, 1996, V. 390, No 3.
pp. 258-260.
17. Popov V.N., Volvenkin S.V., Eprintsev
A.T., Igamberdiev A.U. Induction of glyoxylate
cycle enzymes in various tissues from starving
rats, Izv. Akad Nauk Ser. Biol, 2000, V. 6, pp.
672-678.
18. Popov V.N., Volvenkin S.V., Eprintsev
A.T., Igamberdiev A.U. Glyoxylate cycle
enzymes are present in liver peroxisomes of
alloxan-treated rats, FEBS Lett, 1998, V. 440,
No 1-2, pp. 55-58.
19. Popov V.N., Volvenkin S. V., Kosmatykh
T. A. et al. Induction of a peroxisomal malate
dehydrogenase isoform in liver of starved rats,
Biochemistry (Mosc), 2001, V. 66, No 5, pp.
496-501.
20. Ruchti M., Widmer F. Isocitrate lyase
from germinating soybean cotyledons:
purification and characterization, J. exp. Bot,
1986, V. 37, pp. 1685-1690.
21. Vincenzini M.T., Nerozzi F., Vincieri
F.F., Vanni P. Isolation and properties of
isocitrate lyase from Lupinus seed,
Phytochemistry, 1980, V. 19, No 5, pp. 769-
774.
22. Watanabe S., Yamaoka N., Fukunaga N.,
Takada Y. Purification and characterization of a
cold-adapted isocitrate lyase and expression
analysis of the cold-inducible isocitrate lyase
gene from the psychrophilic bacterium
Colwellia psychrerythraea, Extremophiles,
2002, V. 6, No 5, pp. 397-405.
23. Dingman D.W., Sonenshein A.L.
Purification of aconitase from Bacillus subtilis
and correlation of its N-terminal amino acid
sequence with the sequence of the citB gene, J.
Bacteriol, 1987, V. 169, No 7, pp. 3062-3067.
Published
2019-11-20
How to Cite
Syromyatnikov, M. Y., Eprintsev, A. T., & Popov, V. N. (2019). Using chromatographic methods for the purification of the key enzymes of the glyoxylate cycle from organisms of different taxonomic groups. Sorbtsionnye I Khromatograficheskie Protsessy, 14(6). Retrieved from https://journals.vsu.ru/sorpchrom/article/view/1584
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