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Influence of Amitrole Upon Protein Metabolism in Bean Plants

Published online by Cambridge University Press:  12 June 2017

John C. Brown  and
Mason C. Carter
John C. Brown
Affiliation:
Department of Forestry, Auburn University, Auburn, Alabama
Mason C. Carter
Affiliation:
Department of Forestry, Auburn University, Auburn, Alabama
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Abstract

No effect was shown of 3-amino-l,2,4-triazole (amitrole) upon the incorporation of alanine or histidine into soluble protein in bean (Phaseolus vulgaris L.) hypocotyls grown in darkness. The metabolic derivative of amitrole, β-(3-amino-1,2,4-triazolyl-l-)α-ala-nine (hereinafter referred to as 3-ATAL), also had no effect upon histidine incorporation. Serine incorporation was increased 56% in the presence of amitrole, but this may result from a reduction of endogenous serine pools. No evidence indicates a general disruption of protein synthesis. Activity from amitrole-5-14C was readily incorporated into bean protein, but hydrolysis revealed no 3-ATAL. Most of the activity was recovered as amitrole. Amitrole in the presence of riboflavin and light attacked bovine serum albumin, probably by free radical formation. Hydrolysis of bovine serum albumin revealed mainly amitrole. Apparently, the entry of amitrole into bean protein is by free radical formation.

Type
Research Article
Information
Weed Science , Volume 16 , Issue 2 , April 1968 , pp. 222 - 226
Copyright
Copyright © Weed Science Society of America 

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References

Literature Cited

1. Bartels, P. G. and Wolf, F. F. 1965. The effect of amitrole upon nucleic acid and protein metabolism of wheat seedlings. Physiol. Plantarum 18:361–364.CrossRefGoogle Scholar
2. Benson, A. A., Bassham, J. A., Calvin, M., Goodale, T. C., Haas, V. A., and Stepka, W. 1950. The path of carbon in photosynthesis. V. Paper chromatography of products. J. Amer. Chem. Soc. 72:1710.CrossRefGoogle Scholar
3. Carter, M. C. and Naylor, A. W. 1961. Studies on an unknown metabolic product of 3-amino-l,2,4-triazole. Physiol. Plantarum 14:20–27.CrossRefGoogle Scholar
4. Carter, M. C. 1965. Studies on the metabolic activity of 3-amino-l,2,4-triazole. Physiol. Plantarum 18:1054–1058.CrossRefGoogle Scholar
5. Castelfranco, P. and Brown, M. S. 1963. A hypothesis of amitrole action based on its behavior toward free radical generating system. Weeds 11:116–124.CrossRefGoogle Scholar
6. Hilton, J. L. 1960. Effect of histidine on the inhibitory action of 3-amino-l,2,4-triazole. Weeds 8:392–396.CrossRefGoogle Scholar
7. Hilton, J. L. 1962. Riboflavin nullification of inhibitory actions of 3-amino-l,2,4-triazole on seedling growth. Plant Physiol. 37:238–243.CrossRefGoogle Scholar
8. Hilton, J. L., Kearney, P. C., and Ames, Bruce N. 1965. Mode of action of the herbicide 3-amino-l,2,4-triazole (amitrole) Inhibition of an enzyme of histidine biosynthesis. Arch. Biochem. Biophys. 112:544–547.CrossRefGoogle Scholar
9. Klopotowski, T. and Hulanicka, Danita. 1963. Imidazole glycerol accumulation by yeast resulting from the inhibition of histidine biosynthesis by 3-amino-l,2,4-triazole. Acta Biochem. Polon. 10:209–218.Google Scholar
10. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:265–275.CrossRefGoogle ScholarPubMed
11. Massini, P. 1959. Synthesis of 3-amino-l,2,4-triazoylalanine from 3-amino-l,2,4-triazole in plants. Biochem. Biophys. Acta. 36:548–549.CrossRefGoogle Scholar
12. Massini, P. 1963. Aminotriazolylalanine: A metabolic product of amino triazole from plants. Acta. Bot. Neer. 12:64–72.CrossRefGoogle Scholar
13. Racusen, D. 1958. The metabolism and translocation of 3-amino-l,2,4-triazole in plants. Arch. Biochem. Biophys. 74:106–113.CrossRefGoogle Scholar
14. Shannon, J. C., Hanson, J. B., and Wilson, C. M. Ribonuclease levels in the mesocotyl tissue of Zea Mays as a function of 2,4-dichlorophenoxyacetic acid application. Plant Physiol. 39:804–809.CrossRefGoogle Scholar
15. Siegel, J. N. and Gentile, Arthur C. 1966. Effect of 3-amino-1,2,4-triazole on histidine metabolism in algae. Plant Physiol. 41:670–672.CrossRefGoogle Scholar
16. Weyter, F. W. and Broquist, H. P. 1960. Interference with adenine and histidine metabolism of microorganisms by aminotriazole. Biochem. Biophys. Acta. 40:567–569.CrossRefGoogle ScholarPubMed
17. Williams, A. K., Cox, S. T., and Eagon, R. G. 1965. Conversion of 3-amino-1,2,4-triazole into 3-amino-l,2,4-triazolylala-nine and its incorporation into protein by Escherchia coli . Biochem. Biophys. Res. Commun. 18:250–254.CrossRefGoogle Scholar