Awade A, Metz-Boutigue M H, Le Ret M, Genot G, Amiri I, Burkard G
Institut de Biologie Moléculaire des Plantes, Strasbourg, France.
Biochim Biophys Acta. 1991 Apr 8;1077(2):241-4. doi: 10.1016/0167-4838(91)90064-7.
We have established the complete sequence of the 155 amino acid residues of the pathogenesis-related protein PR2 accumulating in bean leaves treated with a mercuric chloride solution. Bean PR2 whose biological function remains to be elucidated, represents a structurally unfamiliar protein in which sequence arginine, cysteine, methionine and tryptophan residues are missing. This sequence is identical to that of bean PvPR1.
我们已经确定了用氯化汞溶液处理的菜豆叶片中积累的病程相关蛋白PR2的155个氨基酸残基的完整序列。菜豆PR2的生物学功能尚待阐明，它代表一种结构上不常见的蛋白质，其中精氨酸、半胱氨酸、蛋氨酸和色氨酸残基序列缺失。该序列与菜豆PvPR1的序列相同。
