The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.).
A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named 'convicilin' and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003429:Cross Reactions; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000032:analysis; D010940:Plant Proteins / Q000276:immunology / Q000302:isolation & purification*; D010946:Plants, Medicinal; D012639:Seeds / Q000032:analysis*
D000596:Amino Acids; C029781:CVC protein, Pisum sativum; D002241:Carbohydrates; D010940:Plant Proteins; D003488:Cyanogen Bromide