Graham J S, Burkhart W, Xiong J, Gillikin J W
Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403.
Plant Physiol. 1992 Jan;98(1):163-5. doi: 10.1104/pp.98.1.163.
A polypeptide structurally related to the thaumatin family of proteins has been purified from soybean (Glycine max) leaves and the complete amino acid sequence has been determined. The mature protein, which we have termed P21, has a calculated molecular weight of 21,461 and an isoelectric point of 4.6. The soybean protein shows 64% amino acid identity with thaumatin, a sweet-tasting protein found in the West African shrub Thaumatococcus danielli, and as much as 71% identity with thaumatin-like polypeptides present in tobacco and maize.
从大豆(Glycine max)叶片中纯化出一种与奇异果甜蛋白家族结构相关的多肽,并测定了其完整的氨基酸序列。我们将这种成熟蛋白命名为P21,其计算分子量为21,461,等电点为4.6。这种大豆蛋白与奇异果甜蛋白有64%的氨基酸同一性,奇异果甜蛋白是一种在西非灌木植物丹尼氏奇异果中发现的甜味蛋白,并且与烟草和玉米中存在的类奇异果甜蛋白多肽有高达71%的同一性。