Polyploidy and aspartate-transcarbamylase activity in Hippocrepis comosa L.
- 1 June 1980
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 149 (1) , 27-33
- https://doi.org/10.1007/bf00386223
Abstract
The DNA content of plants which were sampled in natural di-, tetra- and hexaploid populations of Hippocrepis comosa L. was estimated and the aspartate transcarbamylase activities of the corresponding cell-free extracts were compared. The amount of DNA is not exactly proportional to the number of genomes. The three kinds of populations do not differ in their aspartate transcarbamylase specific activity. While the enzyme properties are identical in the extracts derived from the diploid and hexaploid plants, the aspartate transcarbamylase present in the tetraploid cytotype shows a slightly lower affinity for one of its substrates and a significantly lower sensitivity to the feedback inhibitor UTP which is still observed after partial purification. These properties might be related to the previously reported greater ability of the tetraploid cytotype to adapt to a variety of biotopes.Keywords
This publication has 19 references indexed in Scilit:
- Le complexe polyploïde de l'hippocrepis comosaL. II. La méioseBulletin de la Société Botanique de France, 1978
- Le complexe polyploïde de l'hippocrepis comosaL. I. La mitoseBulletin de la Société Botanique de France, 1977
- Studies on Plant Aspartate TranscarbamylaseEuropean Journal of Biochemistry, 1974
- Biosynthesis of Escherichia coli aspartate transcarbamylase: I. Parameters of gene expression and sequential biosynthesis of the subunitsJournal of Molecular Biology, 1972
- Aspartate transcarbamoylase from Phaseolus aureus. Partial purification and propertiesBiochemical Journal, 1972
- Nucleic acid content and Chromosome morphology in ChrysanthemumGenetics Research, 1969
- A study of the aspartate transcarbamylase activity of yeastArchives of Biochemistry and Biophysics, 1967
- Aspartic Transcarbamylase from Lettuce Seedlings: Case of End-Product InhibitionNature, 1962
- Absorption microphotometry of irregular-shaped objectsChromosoma, 1953
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934