Homology between legumin-like polypeptides from cereals and pea

Abstract

The presence of legumin-like constituents within the globulin fractions of wheat (Triticum aestivum), rye (Secale cereale) and corn (maize, Zea mays) was demonstrated. Two-dimensional analysis of wheat globulins in the presence and absence of a reducing agent revealed the existence of reducible approximately 60 kDa polypeptides. Western-blot analysis with 125I-labelled antibodies raised against the oat (Avena sativa) 12S globulin holoprotein or its alpha-subunits demonstrated, firstly, the immunological homology between the alpha- and beta-subunits of pea (Pisum sativum) legumin and oat 12S globulin, and secondly, the similar occurrence in wheat of antigenically homologous approximately 20kDa and approximately 40 kDa polypeptides that associate via disulphide linkage to form approximately 60 kDa dimers. Western blotting also showed the presence of disulphide-linked approximately 20 kDa and approximately 40 kDa legumin-like subunits within the globulin fractions of rye and corn.

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

“…To characterize the Glo-3 antigenically-related proteins in whole AC Barrie seeds, globulins were extracted, following the classical method [ 21 , 22 ]. The globulin-enriched fraction was separated by 1D SDS-PAGE and immunoblots were probed with polyclonal rabbit antibodies specific for Glo-3A (Figure 1 ) [ 15 ].…”

Analysis of expressed sequence tags from Actinidia: applications of a cross species EST database for gene discovery in the areas of flavor, health, color and ripening

“…Globulin proteins (11S and 7S) have been reported from a wide range of seeds, including cereals [ 72 , 73 ] and legumes [ 74 ]. Globulin-like proteins are also found in A. thaliana [ 75 ] and a gene family of 10 globulin-like genes are present in Arabidopsis gene databases (The Arabidopsis Information Resource (TAIR), ).…”

Electrophoretic and Immunological Analyses of Almond (Prunus dulcis L.) Genotypes and Hybrids

“…Molecular heterogeneity of storage protein polypeptides within plant species is not uncommon and has been observed in soybean proteins (9,10,26,36,39,49), sesame 11S globulin (43), and several other plant seed storage proteins (11,14,15,21,25,27,28,30,45). Although precise structural differences underlying such polypeptide micro-heterogeneity are not fully established, glycosylation and proteolytic processing (co-and/ or posttranslational) appear to be the main sources of variability (6,25,26).…”