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Purification of a storage protein ofPsophocarpus tetragonolobus

Authors
Journal
Phytochemistry
0031-9422
Publisher
Elsevier
Publication Date
Volume
25
Issue
3
Identifiers
DOI: 10.1016/0031-9422(86)88005-0
Keywords
  • Psophocarpus Tetragonolobus
  • Leguminosae
  • Winged Bean
  • Seed Storage Protein
  • Psophocarpin B1
  • Tuber Storage Protein
  • Radio-Immunoassay
  • Germination
  • Protein Crystals.
Disciplines
  • Biology

Abstract

Abstract Psophocarpin B 1, one of the major seed storage proteins of Psophocarpus tetragonolobus (winged bean), has been purified to homogeneity and crystallized. It is an acidic protein with a pI of 5.5 and M r of 20 000, as determined by gel filtration in the absence of denaturating agents. Polyacrylaniide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS-PAGE), indicates the absence of a quaternary structure of the protein. Using specific antibody raised in rabbits, a radio-immunoassay (RIA) method has been developed for its quantitation. It shows that 12% of the total soluble protein in the tuber of this plant is psophocarpin B 1 whereas it represents 9% of the seed protein. In the pods, it is only a minor component (1% of the total soluble protein) and it is not detectable in stems and leaves. Psophocarpin B 1 undergoes a time-dependent degradation in germinating seeds.

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