Shimokawa Y, Kuromizu K, Araki T, Ohata J, Abe O
Eur J Biochem. 1984 Sep 17;143(3):677-84. doi: 10.1111/j.1432-1033.1984.tb08421.x.
The complete amino acid sequence (72 amino acid residues) of a double-headed proteinase inhibitor from seeds of Vicia angustifolia L. var. segetalis Koch has been determined and compared with those of other double-headed inhibitors of known structure. Sequencing was performed by conventional methods with the aid of the fragments produced by reduction and S-carboxymethylation of the enzymatically modified inhibitors, and also using tryptic and chymotryptic peptides. The positions of the 14 half-cystine residues agreed among all the reported primary structures of the legume double-headed inhibitors. However, V. angustifolia inhibitor possessed extensive amino acid differences compared to the others. The phylogenetic relationship among these inhibitors was established using the unweighted pair-group method and revealed that the V. angustifolia inhibitor and the peanut inhibitor B-III had diverged at a relatively earlier stage compared to the other inhibitors.
窄叶野豌豆变种田野野豌豆种子中一种双头蛋白酶抑制剂的完整氨基酸序列（72个氨基酸残基）已被测定，并与其他已知结构的双头抑制剂进行了比较。测序采用常规方法，借助酶修饰抑制剂还原和S-羧甲基化产生的片段，以及胰蛋白酶和糜蛋白酶肽段。在所有已报道的豆科双头抑制剂一级结构中，14个半胱氨酸残基的位置是一致的。然而，与其他抑制剂相比，窄叶野豌豆抑制剂存在广泛的氨基酸差异。使用非加权配对组法建立了这些抑制剂之间的系统发育关系，结果表明，与其他抑制剂相比，窄叶野豌豆抑制剂和花生抑制剂B-III在相对较早的阶段就发生了分化。
