Molecular and Subunit Heterogeneity of Legumin ofPisum sativumL. (Garden Pea)— A Multi-Dimensional Gel Electrophoretic Study
Narender K. Matta, John A. Gatehouse, Donald Boulter
Abstract
Narender K. Matta, John A. Gatehouse, Donald Boulter
Abstract
Pisum sativum legumin has been shown to be heterogeneous with respect to the existence of different molecular forms, the molecular weights of subunit pairs, and the molecular weights and isoelectric points of constituent subunits. Disulphide-bonded subunit pairs with mol. wt. 54 000 constitute a major part of total legumin. In addition, subunit pairs varying in mol. wt. from 35 000 to 58 000 have been observed which associate in various ways to give rise to at least three distinct molecular forms of legumin separable on non-dissociating gels. ‘Three-dimensional’ gel electro-phoresis has been employed to understand the consitution of these forms in detail.
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Pisum sativum legumin has been shown to be heterogeneous with respect to the existence of different molecular forms, the molecular weights of subunit pairs, and the molecular weights and isoelectric points of constituent subunits. Disulphide-bonded subunit pairs with mol. wt. 54 000 constitute a major part of total legumin. In addition, subunit pairs varying in mol. wt. from 35 000 to 58 000 have been observed which associate in various ways to give rise to at least three distinct molecular forms of legumin separable on non-dissociating gels. ‘Three-dimensional’ gel electro-phoresis has been employed to understand the consitution of these forms in detail.
Key concepts: Legumin, Pisum, Sativum, Protein subunit, Molecular mass, Isoelectric point, Biochemistry, Biology