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LEGUMIN OF PISUM SATIVUM AND VICIA FABA
Author(s) -
CROY R. R. D.,
DERBYSHIRE E.,
KRISHNA T. G.,
BOULTER D.
Publication year - 1979
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1979.tb00723.x
Subject(s) - legumin , vicia faba , pisum , sativum , vicilin , biology , vicia , biochemistry , protein subunit , botany , amino acid , storage protein , gene
S ummary The legumins of Pisum and Vicia have been compared and the proteins have been shown to differ in molecular weight, subunit molecular weights and amino acid composition. Legumin of Pisum however has a similar disulphide bridged subunit construction to that of Vicia and consists of basic (pI's greater than 7) and acidic subunits (pI's less than 7). Of the two molecules, Pisum legumin was shown to be more acidic at pH values of neutral and above. The protein from Pisum has all the antigenic determinants of Vicia legumin and one or more determinant groups in addition. Tryptic peptide maps indicate that legumin is an homologous protein in Vicia and Pisum.