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Enzyme Activities in Prickly Sida (Sida spinosa) Seeds of Different Developmental Stages

Published online by Cambridge University Press:  12 June 2017

E. W. Smith ,
B. J. Reger  and
G. H. Egley
E. W. Smith
Affiliation:
1972 NSF Postdoctoral Intern in the South. Weed Sci. Lab.
B. J. Reger
Affiliation:
South. Weed Sci. Lab., Agric. Res. Serv., U.S. Dep. Agric., Stoneville, MS 38776
G. H. Egley
Affiliation:
South. Weed Sci. Lab., Agric. Res. Serv., U.S. Dep. Agric., Stoneville, MS 38776
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Abstract

Key metabolic enzymes and germination were studied in developing and mature, dormant and nondormant prickly sida (Sida spinosa L.) seeds. Isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, fructose-1,6-diphosphatase, and phosphofructokinase activities were determined in developing and mature prickly sida seeds. Developing seeds less than 7 days after anthesis and at 17 days or greater after anthesis were unable to germinate. The 7-day-old seeds lacked all but fructose-1,6-diphosphatase activity. The 17-day-old seeds demonstrated all enzyme activities but failed to germinate because dehydration had occurred and seeds were unable to imbibe sufficient water without an afterripening period. Comparison of enzyme activities of dormant and nondormant seeds on incubation showed that only glucose-6-phosphate dehydrogenase was considerably different within the first 8 h of incubation. Nondormant seeds had considerable glucose-6-phosphate dehydrogenase activity before germination (radical protrusion at 8 h), suggesting an active pentose phosphate pathway.

Keywords

Germinationdormancymetabolismanthesisafterripening
Type
Research Article
Information
Weed Science , Volume 26 , Issue 4 , July 1978 , pp. 349 - 351
Copyright
Copyright © 1978 by the Weed Science Society of America 

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References

Literature Cited

1. Ashihara, H. and Komamine, A. 1975. The function of the pentose phosphate pathway in Phaseolus mungo hypocotyls. Phytochemistry 14:95–98.Google Scholar
2. Egley, G. H. 1976. Germination of developing prickly sida seeds. Weed Sci. 24:239–243.Google Scholar
3. Kornberg, A. and Pricer, W. E. 1951. Di-and triphosphopyridine nucleotide isocitric dehydrogenases in yeast. J. Biol. Chem. 189:123–136.CrossRefGoogle ScholarPubMed
4. Lam, T. H. and Shaw, M. 1970. Removal of phenolics from plant extracts by grinding with anion exchange resin. Biochem. Biophys. Res. Commun. 39:965–968.Google Scholar
5. 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
6. Marks, P. A. 1966. Glucose 6-Phosphate Dehydrogenase-Clinical Aspects. Pages 131–137 in Colowick, S. P. and Kaplan, N. O., eds. Methods in Enzymology. Academic Press, New York.Google Scholar
7. Mohapatra, N., Smith, E. W., Fites, R. C., and Noggle, G. R. 1970. Chilling temperature depression of isocitratase activity from cotyledons of germinating cotton. Biochem. Biophys. Res. Commun. 40:1253–1258.Google Scholar
8. Reger, B. J. and Smith, E. W. 1976. Development of isocitric lyase activity in germinating prickly sida seed. Weed Sci. 24:298–301.Google Scholar
9. Roberts, E. H. 1972. Oxidative processes in the control of seed germination. Pages 189–218 in Haydecker, W., ed. Seed Ecology. Pennsylvania State Univ. Press, University Park, Pennsylvania.Google Scholar
10. Rosen, O. M., Rosen, S. M., and Horecker, B. L. 1966. Fructose-1,6-diphosphatase. Pages 632–636 in Colowick, S. P. and Kaplan, N. O., eds. Methods in Enzymology. Academic Press, New York.Google Scholar
11. Simmonds, J. A. and Simpson, G. M. 1971. Increased participation of pentose phosphate pathway in response to afterripening and gibberellic acid treatment in caryopses of Avena fatua . Can. J. Bot. 49:1833–1840.Google Scholar
12. Sols, A. and Salas, M. L. 1966. Phosphofructokinase. Pages 436–442 in Colowick, S. P. and Kaplan, N. O., eds. Methods in Enzymology. Academic Press, New York.Google Scholar