Huntingdon Road Laboratories, Plant Breeding Institute, 181A Huntingdon Road, CB3 ODY, Cambridge, UK.
Planta. 1979 Jan;145(1):83-8. doi: 10.1007/BF00379931.
Proteins were extracted from wheat meal or flour in 0.1 M acetic acid, 3 M urea and 0.01 M CTAB and fractionated in columns of cross-linked Sepharose in the same solvent. An heterogeneous fraction of high molecular weight eluted from the column which, when reduced and subjected to SDS-polyacrylamide-gel electrophoresis, separated into 12 components. Their molecular weights ranged from about 31,500 to 136,000. The unreduced protein was insoluble in salt solutions and aqueous ethanol but soluble in 0.1 M acetic acid and was therefore defined as glutenin. Glutenins of different molecular weight were made up from the same subunits but in different proportions. The ethanol-soluble proteins (gliadins) of the flour were fractionated in Sephadex G-100. The protein component that was excluded from the Sephadex gel, often described as high-molecular-weight gliadin, was shown to contain 8 distinguishable subunits and they had identical mobilities to 8 of the 12 subunits of glutenin.
蛋白质从麦麸或面粉中用 0.1 M 乙酸、3 M 尿素和 0.01 M CTAB 提取，用交联琼脂糖凝胶柱在相同溶剂中进行分级分离。从柱上洗脱的高分子量异质部分，经还原后进行 SDS-聚丙烯酰胺凝胶电泳，分离出 12 个成分。它们的分子量范围从约 31500 到 136000。未还原的蛋白质不溶于盐溶液和水乙醇，但溶于 0.1 M 乙酸，因此被定义为麦谷蛋白。不同分子量的麦谷蛋白由相同的亚基组成，但比例不同。面粉中的乙醇可溶性蛋白质（醇溶蛋白）在 Sephadex G-100 中进行分级分离。通常被描述为高分子量醇溶蛋白的不被 Sephadex 凝胶排斥的蛋白质成分，被证明含有 8 个可区分的亚基，它们与麦谷蛋白的 12 个亚基中的 8 个具有相同的迁移率。
