Sind die multiplen Formen der Glutamatdehydrogenase aus Erbsenkeimlingen Conformer?
- 1 January 1972
- journal article
- abstracts
- Published by Springer Nature in Planta
- Vol. 104 (1), 78-88
- https://doi.org/10.1007/bf00387685
Abstract
The multiple molecular forms of glutamate dehydrogenase from pea seedlings (Pisum sativum, var. Späth's Violetta) have been investigated. When protein preparations are subjected to electrophoresis on polyacrylamide gels, the glutamate dehydrogenase can be localized by substrate staining. Shoots show seven activity bands, whereas roots have one main zone and several faint ones. SO2-fumigation generates typical alterations of the shoot zymogram. The molecular weight of all the distinct enzyme components is identical and has been shown to be 210000. Urea denaturation with subsequent renaturation of the various glutamate dehydrogenase preparations from roots, shoots and SO2-fumigated shoots results in the formation of one identical activity band on polyacrylamide gels. The results discussed here give much evidence that the multiple molecular forms of glutamate dehydrogenase from pea seedlings are conformers.Keywords
This publication has 18 references indexed in Scilit:
- Conformers of Neurospora glutamate dehydrogenaseJournal of Molecular Biology, 1969
- The amino acid composition of the subunit of the NADP-specific glutamate dehydrogenase from Neurospora crassaBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- Isoenzymes of Glutamate Dehydrogenase in PlantsPlant Physiology, 1969
- Glutamate deshydrogenase. Structure quaternaire et proprietes rotatoiresEuropean Journal of Biochemistry, 1969
- Sedimentation Coefficient and Molecular Weight of Beef Liver Glutamate Dehydrogenase at the Microgram and the Milligram LevelEuropean Journal of Biochemistry, 1968
- NATURE OF MULTIPLE MOLECULAR FORMS OF ENZYMES*Annals of the New York Academy of Sciences, 1968
- AN APPROACH TO THE PROBLEM OF CONFORMATIONAL ISOZYMESAnnals of the New York Academy of Sciences, 1968
- Molecular weight of the subunits, oligomeric and associated forms of bovine liver glutamate dehydrogenaseJournal of Molecular Biology, 1968
- Enzymes involved in Glutamate Metabolism in Legume Root NodulesNature, 1966
- Isoenzymatic Nature of L-Glutamic Dehydrogenase of Higher PlantsNature, 1965