SDS-insoluble glutenin polymer formation in developing grains of hexaploid wheat: the role of the ratio of high to low molecular weight glutenin subunits and drying rate during ripening

The accumulation of polymeric proteins and the changes in molecular size distribution of these proteins were followed during grain filling and/or premature desiccation. The accumulation behavior of polymeric proteins and their constituent polypeptides (high and low molecular weight glutenin subunits, HMW-GS and LMW-GS) was determined by reversed phase-high performance liquid chromatography using a NaI/propanol purification procedure. With this new extraction and separation procedure, we have demonstrated that there was a coordinated initiation of storage protein biosynthesis, even if the accumulation rate varied greatly between the two main classes of proteins (i.e. monomeric and polymeric fractions). Moreover, the glutenin subunit composition was largely modified during glutenin accumulation. Both the HMW-GS/LMW-GS and HMW-GS-x/HMW-GS-y ratios increased significantly during the whole cell enlargement phase (from 16 to 37 d after anthesis). By applying premature grain desiccation during this physiological phase, we demonstrated that the polymerization index (SDS-insoluble polymers/total polymers) of the glutenin polymers was closely related to the HMW-GS/LMW-GS ratio of these proteins. An increase in the relative proportion of HMW-GS in glutenins caused the proportion of SDS-insoluble polymers to rise during grain desiccation. From these studies, it appears that the modification of the desiccation rate (grain desiccation at a constant temperature with variable relative humidity levels) induced a parallel modification of the glutenin insolubilization rate but did not affect the polymerization index of the glutenins at maturity.