Federal Research, Science and Education Administration, United States Department of Agriculture, and Department of Agronomy, University of Wisconsin, Madison, Wisconsin 53706.
Plant Physiol. 1978 Oct;62(4):506-9. doi: 10.1104/pp.62.4.506.
Oat (Avena sativa L.) seed globulin was extracted from ground caryopses with 1 m NaCl, 0.05 m Tris(hydroxymethyl)aminoethane (pH 8.5) at room temperature. The globulin had a sedimentation constant of 12.1, and a molecular weight of 322,000, as determined by analytical ultracentrifugation. The globulin could be separated into two major subunits by sodiumdodecyl sulfate polyacrylamide gel electrophoresis. Molecular weights of the subunits were 21,700 (alpha) and 31,700 (beta), and they were present in equimolar amounts. A subunit model of 6alpha and 6beta per molecule of globulin is proposed. Amino acid analysis indicated that the alpha subunit contained more basic amino acids and aspartic acid/asparagine but less glutamic acid/glutamine and glycine than the beta subunit.
燕麦球蛋白（Avena sativa L.）从粉碎的麦粒中用 1 m NaCl 和 0.05 m Tris(hydroxymethyl)aminoethane（pH 8.5）在室温下提取。球蛋白经分析超速离心法测定，沉降常数为 12.1，分子量为 322,000。球蛋白经十二烷基硫酸钠聚丙烯酰胺凝胶电泳可分为两个主要亚基。亚基分子量分别为 21,700（α）和 31,700（β），两者含量相等。提出球蛋白每个分子有 6α和 6β个亚基的亚基模型。氨基酸分析表明，α亚基比β亚基含有更多的碱性氨基酸和天门冬氨酸/天冬酰胺，但谷氨酸/谷氨酰胺和甘氨酸较少。
