Skip to main content
Log in

A study on the inhibition of rat myocardium glutathione peroxidase and glutathione reductase by moniliformin

  • Published:
Mycopathologia Aims and scope Submit manuscript


In preparations of Wistar rat myocardium, Km values of GSH-Px to the substrates, H2O2 and GSH, as determined by the DTNB method, were 1.9×10−4 mol/L and 2.0×10−3 mol/L respectively. The Km value of GSSG-R to GSSG was 6.0×10−5 mol/L by UV spectrophotometric assay. In vitro, the activity of GSH-Px was inhibited by 1.0, 6.0 and 16.0 mmol/L synthetic moniliformin (MF) with the corresponding activities of 89.4%, 65.2% and 47.9% of control values (n=6). The activities of GSSG-R in the presence of 16.0 and 32.0 mmol/L MF were 74.4% and 61.9% of controls (n=5) respectively. These results revealed that the inhibition of GSH-Px by MF was stonger than that of GSSG-R. As determined by Lineweaver-Burk and of Dixon plots, the inhibition of GSH-Px and GSSG-R by MF was competitive and noncompetitive, respectively. The affinity of GSH-Px to MF was higher than that of GSSG-R because the inhibition constant Ki of the former (6.0 mmol/L) was less than that of the latter (39 mmol/L). We suggest that the mechanism of toxic-damaging effects of MF on myocardium, may be closely related to the failure of remove of free radicals by some enzymes, as GSH-Px and GSSG-R, and that MF may be involved in keshan disease.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others


  1. Thiel PG. A molecular mechanism for the toxic action of moniliformin, a myocotoxin produced by Fusarium moniliforme. Biochem Pharmac 1978; 27: 483–6.

    Google Scholar 

  2. Zhang H, Li JL. Study on toxicological mechanism of moniliformin, Acta Microbiologica Sinica 1989; 29: 91–100.

    Google Scholar 

  3. Kriek NPJ, Marasas WFO, Steyn PS, van Rensburg SJ, Steyn M. Toxicity of a moniliformin-producing strain of Fusarium moniliforme var. Subglutinans isolated from maize. Fd Cosmet Toxicol 1977; 15: 579–87.

    Google Scholar 

  4. Yang GQ, Wang GY, Yin TA. Relationship between the distribution of Keshan disease and selenium status. Acta Nutr Sinica 1982; 4: 191–8.

    Google Scholar 

  5. Yu Wei-han (editor). Studies on prevention and treatment of Chinese Keshan disease. P.180, 1987 (in Chinese).

  6. Yu Wei-han (editor). Studies on prevention and treatment of Chinese Keshan disease. P.216, 1987 (in Chinese).

  7. Zhu LZ, Xia YM, Yang GQ. Blood glutathione peroxidase activities of populations in Keshan disease affected and non-affected areas. Acta Nutr Sinica 1982; 4: 229–33.

    Google Scholar 

  8. Yu Wei-han (editor). Studies on prevention and treatment of Chinese Keshan disease. P.233, 1987 (in Chinese).

  9. Myers CL, Weiss SJ, Kirsh MM, Shlafer M. Involvement of hydrogen peroxide and hydroxyl radical in the oxygen paradox: reduction of creatine kinase by catalase, allopurinol or deferoxamine but not by superoxide dismutase. J Mol Cell Carbiol 1985; 17: 675–84.

    Google Scholar 

  10. Chen LY. The membrane and some pathologic changes in myocardium. Physiol Sci 1988; 3: 265–70.

    Google Scholar 

  11. Li FS, Zou LM, Duan YJ. The effect of phospholipid metabolism on structure and function of membrane bound enzymes from the myocardium of guinea pigs. Acta Biochem Biphys Sinica 1984; 16: 694–7.

    Google Scholar 

  12. Belluš D, Fisher H, Greuter H, Martin P. Synthesen von moniliformin, einem mycotoxin mit cyclobutendionstruktur. Helvetica. Chimica Acta 1978; 61: 1784–813.

    Google Scholar 

  13. Hafeman DG, Sunde RA, Hoekstra WG. Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat. J Nutr 1974; 104: 580–7.

    Google Scholar 

  14. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265–75.

    Google Scholar 

  15. Paglia DE, Valentine EN. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase 1967; 70: 158–69.

    Google Scholar 

  16. Wolff SP, Garner A, Dean RT. Free radicals, lipids and protein degradation. TIBS 1986; 11: 27–31.

    Google Scholar 

  17. Guo KD. On theory of mycotoxin-intoxication as etiology of Keshan disease. In Yamaguchi H, Ogawa H, Migaji M, eds. Proceedings of the first China-Japan international congress of mycology, Tokyo, 1987; 148–9.

Download references

Author information

Authors and Affiliations


Rights and permissions

Reprints and permissions

About this article

Cite this article

Chen, L.Y., Tian, X.L. & Yang, B. A study on the inhibition of rat myocardium glutathione peroxidase and glutathione reductase by moniliformin. Mycopathologia 110, 119–124 (1990).

Download citation

  • Revised:

  • Accepted:

  • Issue Date:

  • DOI:

Key words