Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 52, Issue 10, Pages 3141-3148Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf035104i
Keywords
Pisum; storage proteins; purification; vicilin; convicilin; subunit composition; heterogeneity
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Vicilin, a major globulin protein of pea that has been described as extremely heterogeneous in terms of its polypeptide composition, was extracted from pea flour under alkaline conditions and subsequently fractionated by salt under acid conditions. This procedure induced the separation of vicilin into two fractions, which, after purification, were called vicilin 1degrees and vicilin 2degrees. Vicilin 2degrees was seen on SDS-PAGE to contain the third globulin protein of pea, convicilin (a band at similar to70 kDa). Vicilin fractions were thus characterized using gel electrophoresis, differential scanning calorimetry, circular dichroism, and pH-dependent solubility in order to determine whether the convicilin should in fact be considered as a third separate globulin protein of pea. On the basis of the results obtained it was concluded that this distinct polypeptide of the Pisum vicilin gene family should be further denoted as a subunit of the salt extractable protein vicilin. The definition of vicilin heterogeneity should therefore be extended to acknowledge the possible oligomeric inclusion of the 70 kDa polypeptide that is here denoted as the alpha-subunit.
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