| Home | E-Submission | Sitemap | Contact us |  
Korean J Parasitol > Volume 21(1):1983 > Article

Original Article
Korean J Parasitol. 1983 Jun;21(1):41-48. English.
Published online Mar 20, 1994.  http://dx.doi.org/10.3347/kjp.1983.21.1.41
Copyright © 1983 by The Korean Society for Parasitology
Aspartate and alanine aminotransferase in Fasciola hepatica
Sun Hyo Park,Nyon Soo Kwon,Hi Sung Lee and Chul Yong Song
Department of Biochemistry, College of Medicine, Chung-Ang University, Korea.
Department of Biology, College of Liberal Arts and Sciences, Chung-Ang University, Korea.

The activity and distribution of aspartate aminotransferase (EC and alanine aminotransferase (EC in adult Fasciola hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows;

1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1 g of Fasciola hepatica, respectively.

2. The activity of those enzymes was relatively low compared with those in mammalian tissues.

3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71% of the activity was in cytosolic, 24% in mitochondrial and 5% was in nuclear fraction.

4. About 22% of the total alanine aminotransferase activity was found in the mitochondrial fraction, about 66% in the cytosolic fraction.

5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.


Fig. 1
Chromatography of GOT on DEAE-cellulose. (•-•, protein; ○-○, enzyme activity).

Fig. 2
Chromatography of GPT on DEAE-cellulose. (•-•, protein; ○-○, enzyme activity).


Table 1
Distribution of aspartate aminotransferase (GOT) in Fasciola hepatica

Table 2
Distribution of GPT from Fasciola hepatica

Table 3
Isozyme patterns of aspartate aminotransferase from Fasciola hepatica

Table 4
Purification of aspartate aminotransferase from Fasciola hepatica

Table 5
Purification of alanine aminotransferase from Fasciola hepatica

1. Agatsuma T, Suzuki N. Electrophoretic studies on enzymes in the Japanese common liver fluke, Fasciola sp. I. Enzyme variations in the natural population. Jpn J Med Sci Biol 1980;33(5):249–254.
2. Agress CM. Am J Cardicl 1959;3:74–82.
3. Augustinsson KB, Erne K. The heterogeneity of serum glutamic-oxalacetic transaminase of certain mammalian species. Experientia 1961;17:396–397.
4. Beaton GH, Curry DM, Veen MJ. Alanine-glutamic transaminase activity and protein metabolism. Arch Biochem Biophys 1957;70(1):288–290.
5. Boyd JW. The extraction and purification of two isoenzymes of L-aspartate:2-oxoglutarate aminotransferase. Biochim Biophys Acta 1966;113(2):302–311.
6. Chen SH, Giblett ER. Polymorphism of soluble glutamic-pyruvic transaminase: a new genetic marker in man. Science 1971;173(992):148–149.
7. Delorenzo RJ, et al. Biochem Genetics 1970;4:259–268.
8. Daugherty JW. Exp Parasitol 1952;1:331–338.
9. DeRosa G, Swick RW. Metabolic implications of the distribution of the alanine aminotransferase isoenzymes. J Biol Chem 1975;250(20):7961–7967.
10. Dixon M. A nomogram for ammonium sulphate solutions. Biochem J 1953;54(3):457–458.
11. Felig P. Amino acid metabolism in man. Annu Rev Biochem 1975;44:933–955.
12. Fleisher GA, et al. Proc Soc Exptl Biol Med 1960;103:229–231.
13. Gutfreund H, Ebner KE, Mendiola L. Transamination and the control of mitochondrial pathways. Nature 1961;192:820–823.
14. Hopper S, Segal HL. Comparative Properties of Glutamic-Alanine Transaminase From Several Sources. Arch Biochem Biophys 1964;105:501–505.
15. Ishimoto G, et al. Jpn Hum Genet 1974;18:373–381.
16. Janssens PA, et al. Comp Biochem Physiol 1969;30:261–272.
17. Kanfer E, et al. Exptl Cell Res 1961;22:120–126.
18. Kopelovich L, Sweetman L, Nisselbaum JS. Time-dependent inhibition of aspartate aminotransferase isozymes by DL-glyceraldehyde 3-phosphate. J Biol Chem 1970;245(8):2011–2017.
19. Kopelovich L, Sweetman L, Nisselbaum JS. Regulation of aspartate aminotransferase isozymes by D-erythrose 4-phosphate and glycolaldehyde phosphate, the naturally occurring homologues of D-glyceraldehyde 3-phosphate. J Biol Chem 1972;247(10):3262–3268.
20. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951;193(1):265–275.
21. Mansour TE. Effect of serotonin on glycolysis in homogenates from the liver fluke Fasciola hepatica. J Pharmacol Exp Ther 1962;135:94–101.
22. Mansour TE. The effect of serotonin and related compounds on the carbohydrate metabolism of the liver fluke, Fasciola hepatica. J Pharmacol Exp Ther 1959;126(3):212–216.
23. Morino Y, et al. Biochem Biophys Res Commun 1963;13:348–352.
24. Moss GD. The excretory metabolism of the endoparasitic digenean Fasciola hepatica and its relationship to its respiratory metabolism. Parasitology 1970;60(1):1–19.
25. Ogawa K, Ichihara A. Isozyme patterns of branched-chain amino acid transaminase in various rat hepatomas. Cancer Res 1972;32(6):1257–1263.
26. Ogawa K, Yokojima A, Ichihara A. Transaminase of branched chain amino acids. VII. Comparative studies on isozymes of ascites hepatoma and various normal tissues of rat. J Biochem 1970;68(6):901–911.
27. Prichard RK, Schofield PJ. A comparative study of the tricarboxylic acid cycle enzymes in Fasciola hepatica and rat liver. Comp Biochem Physiol 1968;25(3):1005–1019.
28. Reed RE, Hess JL. Partial purification and characterization of aspartate aminotransferases from seedling oat leaves. J Biol Chem 1975;250(12):4456–4461.
29. Rehfeld DW, Tolbert NE. Aminotransferases in peroxisomes from spinach leaves. J Biol Chem 1972;247(15):4803–4811.
30. Rosen F, Roberts NR, Nichol CA. Glucocorticosteroids and transaminase activity. I. Increased activity of glutamicpyruvic transaminase in four conditions associated with gluconeogenesis. J Biol Chem 1959;234(3):476–480.
31. Saier MH Jr, Jenkins WT. Alanine aminotransferase. I. Purification and properties. J Biol Chem 967 Jan;242(1):91–100.
32. Schimke RT. Adaptive characteristics of urea cycle enzymes in the rat. J Biol Chem 1962;237:459–468.
33. Shrago E, Lardy HA. Paths of carbon in gluconeogenesis and lipogenesis. II. Conversion of precursors to phosphoenolpyruvate in liver cytosol. J Biol Chem 1966;241(3):663–668.
34. Swick RW, Barnstein PL, Stange JL. The Metabolism Of Mitochondrial Proteins. I. Distribution And Characterization Of The Isozymes Of Alanine Aminotransferase In Rat Liver. J Biol Chem 1965;240:3334–3340.
35. Swick RW, Barnstein PL, Stange JL. The Metabolism Of Mitochondrial Proteins. II. The Response Of The Isozymes Of Alanine Aminotransferase To Diet And Hormones. J Biol Chem 1965;240:3341–3345.
36. Taylor RT, Jenkins WT. Leucine aminotransferase. II. Purification and characterization. J Biol Chem 1966;241(19):4396–4405.
37. Zuchlewski AC, Gaebler OH. Changes in the activity of transaminases and L-glutamic acid dehydrogenase induced by growth hormone. Arch Biochem Biophys 1957;66(2):463–473.
Editorial Office
c/o Department of Medical Environmental Biology
Chung-AngUniversity College of Medicine, Dongjak-gu, Seoul 06974, Korea
Tel: +82-2-820-5683   Fax: +82-2-826-1123   E-mail: kjp.editor@gmail.com
About |  Browse Articles |  Current Issue |  For Authors and Reviewers
Copyright © 2018 by The Korean Society for Parasitology and Tropical Medicine. All rights reserved.     powerd by m2community