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The sodium dodecylsulphate (SDS) binding capacities of secalin, gliadin and gluten in the presence of a very low SDS concentration were determined and compared to the SDS binding capacities of bovine serum albumin (BSA), beta-lactoglobulin, ovalbumin und beta-casein. The SDS binding capacities of endosperm proteins determined in phosphate buffer (pH 6.0) are very low. Only 0.6 microgram .. 0.8 microgram SDS were bound to 500 micrograms of the proteins. This low SDS binding capacities do not correlate with the expected hydrophobicity of these proteins. In comparison, 500 micrograms of ovalbumin, beta-lactoglobulin and BSA each bind 0.5, 5.9 and 13.5 micrograms SDS, respectively. According to literature the SDS binding capacities of these proteins are in correlation with the surface hydrophobicity determined with cis-parinaric acid using the fluorescence probe method. The SDS binding capacities of endosperm proteins increased in the presence of 0.1 N acetic acid and consequently 6.2 micrograms .. 6.9 micrograms SDS were bound to 500 micrograms of the corresponding proteins. beta-casein described as a highly hydrophobic protein binds only 0.9 micrograms SDS to 500 micrograms of it in phosphate puffer (pH 6.0) and 1.2 micrograms SDS in 0.1 N acetic acid, respectively. |
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