Mendoza E M, Adachi M, Bernardo A E, Utsumi S
Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.
J Agric Food Chem. 2001 Mar;49(3):1552-8. doi: 10.1021/jf001041h.
Vicilin type (8S) and basic 7S globulins and legumin type (11S) globulins were isolated from mungbean [Vigna radiata (L.) Wilczek]. The native molecular weights of the different globulin types were 360000 for legumin, 200000 for vicilin, and 135000 for basic 7S. Some of the 8S globulin apparently complexed and coeluted with the 11S on gel filtration. On SDS-PAGE, 11S was composed of two bands of 40000 and 24000, 8S was composed of 60000, 48000, 32000, and 26000 bands, and basic 7S was composed of 28000 and 16000 bands. The percent composition of total globulins was estimated to be as follow: 8S, 89%; basic 7S, 3.4%; and 11S, 7.6%. The basic 7S and 11S but not the 8S globulins were found to have disulfide bonds. The presence of carbohydrates by conjugated peroxidase reaction was observed in all bands of 8S, the acidic polypeptide of basic 7S, and its complex but not in 11S. The 28000 basic 7S band and its 42000 complex and the first three major bands of 8S cross-reacted with antibodies to all types of soybean conglycinin subunits (alpha, alpha', and beta), whereas the fourth band cross-reacted only with the anti-beta subunit. None of the mungbean globulins cross-reacted with anti-soybean glycinin. Basic 7S was found to be easily extracted with 0.15 M NaCl, 11S was extracted with 0.35 M NaCl,and 8S was extracted over a wide range of NaCl concentrations. The N-terminal sequences of the different subunits/fragments of the globulins were determined and found to have strong homology with storage proteins of other legumes and crops.
从绿豆[Vigna radiata (L.) Wilczek]中分离出了豌豆球蛋白类型（8S）、碱性7S球蛋白和豆球蛋白类型（11S）球蛋白。不同球蛋白类型的天然分子量分别为：豆球蛋白360000、豌豆球蛋白200000、碱性7S球蛋白135000。在凝胶过滤中，部分8S球蛋白显然与11S球蛋白复合并同时洗脱。在SDS-PAGE上，11S由40000和24000两条带组成，8S由60000、48000、32000和26000条带组成，碱性7S由28000和16000条带组成。总球蛋白的百分比组成估计如下：8S，89%；碱性7S，3.4%；11S，7.6%。发现碱性7S和11S球蛋白含有二硫键，而8S球蛋白不含。通过共轭过氧化物酶反应观察到，在8S的所有条带、碱性7S的酸性多肽及其复合物中存在碳水化合物，但在11S中不存在。28000的碱性7S条带及其42000的复合物以及8S的前三条主要条带与所有类型大豆伴球蛋白亚基（α、α'和β）的抗体发生交叉反应，而第四条带仅与抗β亚基发生交叉反应。绿豆球蛋白均未与抗大豆球蛋白发生交叉反应。发现碱性7S球蛋白很容易用0.15 M NaCl提取，11S球蛋白用0.35 M NaCl提取，8S球蛋白在很宽的NaCl浓度范围内均可提取。测定了球蛋白不同亚基/片段的N端序列，发现它们与其他豆类和作物的贮藏蛋白具有高度同源性。
