印加花生（Plukenetia volubilis L.）蛋白的增溶、分级和电泳特性。
Solubilization, fractionation, and electrophoretic characterization of Inca peanut (Plukenetia volubilis L.) proteins.
机构信息
Department of Nutrition, Food & Exercise Sciences, College of Human Sciences, The Florida State University, Tallahassee, FL 32306-1493, USA.
出版信息
Plant Foods Hum Nutr. 2012 Sep;67(3):247-55. doi: 10.1007/s11130-012-0301-5.
Effects of different solvents, ionic strength, and pH on Inca peanut seed protein solubility were assessed by quantitatively analyzing solubilized proteins using Lowry and Bradford methods. Soluble proteins were fractionated using Osborne procedure and the polypeptide composition of solubilized proteins was determined by one dimensional 25 % monomer acrylamide linear gradient SDS-PAGE. Osborne protein fractions were analyzed by the 2D gel electrophoresis. Total seed proteins were efficiently solubilized by 2 M NaCl among the tested solvents. The soluble seed proteins registered a minimum solubility at pH ~4.0. Osborne protein fractions, albumins, globulins, prolamins, and glutelins accounted for 43.7, 27.3, 3.0, and 31.9 %, respectively, of the total aqueous soluble proteins. Soluble seed flour proteins are mainly composed of polypeptides in the MW range of 6-70 kDa of which the predominant polypeptides were in the 20-40 kDa range. Prolamin fraction was mainly composed of four polypeptides (MW < 15 kDa). Glycoprotein staining indicated 32-35 and <14 kDa peptides to be positive.
采用 Lowry 和 Bradford 法定量分析溶解蛋白，评估了不同溶剂、离子强度和 pH 值对印加花生种子蛋白溶解度的影响。采用 Osborne 法对可溶性蛋白进行分级，通过一维 25%单体丙烯酰胺线性梯度 SDS-PAGE 测定溶解蛋白的多肽组成。采用 2D 凝胶电泳分析 Osborne 蛋白级分。在测试的溶剂中，2 M NaCl 可有效溶解全部种子蛋白。可溶性种子蛋白在 pH 值~4.0 时溶解度最低。Osborne 蛋白级分、白蛋白、球蛋白、醇溶蛋白和谷蛋白分别占总水溶蛋白的 43.7%、27.3%、3.0%和 31.9%。可溶性种子粉蛋白主要由 MW 为 6-70 kDa 的多肽组成，其中主要的多肽在 20-40 kDa 范围内。醇溶蛋白级分主要由四个 MW<15 kDa 的多肽组成。糖蛋白染色表明 32-35 kDa 和<14 kDa 的肽段为阳性。
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