Plant Foods for Human Nutrition

, Volume 33, Issue 2, pp 227–229

Physicochemical and structural studies of phaseolin from French bean seed

Authors

  • R. J. Blagrove
    • CSIRO Division of Protein Chemistry
  • P. M. Colman
    • CSIRO Division of Protein Chemistry
  • G. G. Lilley
    • CSIRO Division of Protein Chemistry
  • A. Van Donkelaar
    • CSIRO Division of Protein Chemistry
  • E. Suzuki
    • CSIRO Division of Protein Chemistry
Article

DOI: 10.1007/BF01091313

Cite this article as:
Blagrove, R.J., Colman, P.M., Lilley, G.G. et al. Plant Food Hum Nutr (1983) 33: 227. doi:10.1007/BF01091313

Abstract

Phaseolin, the main reserve globulin in seeds of the French bean (Phaseolus vulgaris L.), has been purified for sedimentation equilibrium analysis. The major protomer at neutral pH has a molecular weight of 150 000±5 000 which associates to a tetrameric form of molecular weight 596 000±20 000 at pH 4.5. The trimeric nature of the protomer is apparent from protein crosslinking experiments. Initial structural studies were made using optical rotatory dispersion and circular dichroism measurements. Two different crystal forms of the protein have been grown and characterised by X-ray diffraction; one of these forms appears suitable for high resolution X-ray analysis.

Key words

French beanPhaseolus vulgarisphaseolinseed globulinseed storage protein
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Copyright information

© Martinus Nijhoff/Dr W. Junk Publishers 1983