The Structure of Legumin ofVicia fabaL.—a Reappraisal
- 1 February 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Experimental Botany
- Vol. 32 (1) , 183-197
- https://doi.org/10.1093/jxb/32.1.183
Abstract
Two-dimensional electrophoretic studies have shown a wide range of heterogeneity in the subunits of legumin isolated from seeds of Vicia faba L. As many as 10 disulphide-linked subunit pairs in the mol. wt. range 37 000–79 000 have been observed. Each subunit pair separated on reduction by 2-mercaptoethanol into a large acidic and a small basic subunit, each of which was shown to be heterogeneous in charge by isoelectric focusing. More heterogeneity was found in the large subunits (mol. wt. range 23 000–58 000; pl range 4.6–6.1) than in the small subunits (mol. wt. range 21 000–23 000; pl range 8.2–8.5). Most legumin molecules seemed to be formed by random association of subunit pairs, although one subunit pair associated only with itself to give a molecular type separable under non-dissociating conditions.This publication has 5 references indexed in Scilit:
- The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)Biochemical Journal, 1980
- Heterogeneity of broad bean leguminBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Isoelectric-focusing properties and carbohydrate content of pea (Pisum sativum) leguminBiochemical Journal, 1980
- Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.)Planta, 1980
- LEGUMIN OF PISUM SATIVUM AND VICIA FABANew Phytologist, 1979