Zhang Y, Luo S, Tan F, Qi Z, Xu L, Zhang A
Sci Sin B. 1982 Mar;25(3):268-77.
The mung bean trypsin inhibitor has been found to be microheterogeneous at N-terminal region due to the presence of several isomers. After treatment with aminopeptidase M it becomes homogeneous and is suitable for sequence determination. Based on the determination of the structures of two active fragments the complete amino acid sequence of mung bean trypsin inhibitor has been elucidated. It consists of 72 amino acid residues with 7 pairs of disulfide bonds. The results show that this inhibitor belongs to the Bowman-Birk inhibitor family.
由于存在几种异构体，已发现绿豆胰蛋白酶抑制剂在N端区域存在微不均一性。用氨肽酶M处理后，它变得均一，适合进行序列测定。基于对两个活性片段结构的测定，已阐明了绿豆胰蛋白酶抑制剂的完整氨基酸序列。它由72个氨基酸残基组成，有7对二硫键。结果表明，这种抑制剂属于鲍曼-伯克抑制剂家族。
