Biochemical and genetic characterization of a monomeric storage protein (T1) with an unusually high molecular weight in Triticum tauschii.

The protein named T1, present in Triticum tauschii, was previously characterized as a high-molecular-weight (HMW) glutenin subunit with a molecular size similar to that of the y-type glutenin subunit-10 of Triticum aestivum. This protein was present along with other HMW glutenin subunits named 2(t) and T2, and was considered as part of the same allele at the Glu-D (t) 1locus of T. tauschii.

Electrophoretic characterisation of fractions collected from gluten protein extracts subjected to size-exclusion high-performance liquid chromatography.

The electrophoretic analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE; reduced and unreduced) of fractions, collected from a size exclusion-high performance liquid chromatography (SE-HPLC) separation of gluten proteins using a column with pore size of around 400A, showed clear resolution for the seven elution ranges studied in two Australian bread wheat lines. Polymeric proteins - high molecular weight (HMW) glutenin subunits, low molecular weight (LMW) glutenin subunits, HMW albumins and some modified omega-gliadins - appeared exclusively in the region within the first peak of the chromatogram (fractions 1 to 5), the limit being a region that resolved as a small peak before the large peak of gliadins and where some omega-gliadins eluted. A larger proportion of HMW glutenin subunits and B subunits contributed to polymer formation of higher molecular weight.

Distinction between genotypes of Lupinus species by sodium dodecyl sulphate-gel electrophoresis and by capillary electrophoresis.

Effective distinction was achieved among a wide range of lupin grain samples by either sodium dodecyl sulphate (SDS)-gel electrophoresis or capillary electrophoresis, based on grain-protein composition. Capillary electrophoresis was faster (< 1 h) and provided slightly greater distinction between the samples. On the other hand, SDS-gel electrophoresis could provide a greater through-put of samples in a 24 h period.

Spread monolayers of proteins.

The study of spread monolayers of proteins is of interest for understanding the fundamental behavior of proteins as well as the many phenomena resulting from their ubiquitous presence at interfaces in nature. Spread monolayers of proteins is a branch of the developing field of membrane mimetic chemistry. In recent times, it has been somewhat neglected in comparison to other branches (such as bilayers, liposomes and vesicles), despite the unique advantage that the arrangement and packing of molecules in monolayers may be measured and controlled.