
TY  - JOUR
A1  - Thomson, JA 
A1  - Schroeder, HE 
T1  - Cotyledonary Storage Proteins in Pisum Sativum. II. Hereditary Variation in Components of the Legumin and Vicilin Fractions
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 1978
VL  - 5
IS  - 3
SP  - 281
EP  - 294
KW  - 
UR  - https://doi.org/10.1071/PP9780281 
N2  - Gel electrophoresis has been used to investigate genetically controlled variation in storage-protein constituents forming five series of bands (LA-LE) derived from legumin fractions, and three series of bands (VA-VC) from vicilin fractions, of pea seeds. In each variant system, the phenotypes of the storage-protein polypeptides from F1 seeds were additive with respect to the band patterns of the parental lines, and identical in reciprocal crosses. Neither dominance nor formation of new interaction products was observed.    Variation in the three systems involving vicilin polypeptides and two of those involving legumin components was found to be based on allelic alternatives at single loci designated Vicilin A (Vca), Vicilin B (Vcb), Vicilin C (Vcc), Legumin A (Lga) and Legumin C (Lgc). For each of these variant systems, the gene products involved and the basis of the phenotypic variation have been discussed. Variants of the VC band complex, in which mobility of two bands both composed of 12 and 14 kdalton polypeptides is altered, appear likely to correspond to vicilin variants described previously. Type lines are specified for each of the variant phenotypes analysed, and for the genes designated. 
ER  -

