Title
Characterization of Pea Vicilin. 1. Denoting Convicilin as the α-Subunit of the Pisum Vicilin Family
Author
O'Kane, F.E.
Happe, R.P.
Vereijken, J.M.
Gruppen, H.
van Boekel, M.A.J.S.
TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
Publication year
2004
Abstract
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 1° and vicilin° 2°. Vicilin 2° was seen on SDS-PAGE to contain the third globulin protein of pea, convicilin (a band at ∼70 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 α-subunit.
Subject
Nutrition
Food technology
Convicillin
Heterogeneity
Pisum
Purification
Storage proteins
Subunit composition
Vicilin
Convicilin
Globulin
Oligomer
Polypeptide
Unclassified drug
Vegetable protein
Vicilin
Vicilin 1
Vicilin 2
Acidity
Alkalinity
Alpha chain
Circular dichroism
Differential scanning calorimetry
Extraction
Flour
Fractionation
Multigene family
Nonhuman
Pea
PH
Polyacrylamide gel electrophoresis
Protein analysis
Protein family
Protein purification
Separation technique
Solubility
Calorimetry, Differential Scanning
Chemical Fractionation
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Peas
Plant Proteins
Protein Structure, Secondary
Solubility
Pisum
Pisum sativum
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DOI
https://doi.org/10.1021/jf035104i
TNO identifier
237770
ISSN
0021-8561
Source
Journal of Agricultural and Food Chemistry, 52 (10), 3141-3148
Document type
article