植物胰蛋白酶抑制剂、α-淀粉酶抑制剂与哺乳动物胰腺分泌型胰蛋白酶抑制剂（卡扎尔型）之间可能的进化关系。
A possible evolutionary relationship between plant trypsin inhibitor, alpha-amylase inhibitor, and mammalian pancreatic secretory trypsin inhibitor (Kazal).
作者信息
Odani S, Koide T, Ono T
出版信息
J Biochem. 1983 Jun;93(6):1701-4. doi: 10.1093/oxfordjournals.jbchem.a134311.
The amino acid sequence of the carboxyl-terminal half of barley trypsin inhibitor was found to be significantly similar to the whole sequence of bovine pancreatic secretory trypsin inhibitor (Kazal). Kazal type inhibitors and related proteins are known for the extraordinary mode of divergence among animals, and the present observation extends this to a plant for the first time. The present observation together with our previous finding of sequence homology between barley trypsin inhibitor and wheat alpha-amylase inhibitor (Odani, S., Koide, T., & Ono, T. (1982) FEBS Lett. 141, 279-282) suggest an unusual evolutionary relationship between cereal enzyme inhibitors and animal proteinase inhibitors of the Kazal type.
已发现大麦胰蛋白酶抑制剂羧基末端一半的氨基酸序列与牛胰分泌性胰蛋白酶抑制剂（卡扎尔型）的完整序列显著相似。卡扎尔型抑制剂及相关蛋白以动物间独特的分化模式而闻名，目前的观察首次将此扩展到了植物。目前的观察结果以及我们之前发现的大麦胰蛋白酶抑制剂与小麦α淀粉酶抑制剂之间的序列同源性（小谷修、小出敏、小野哲（1982年）《欧洲生物化学学会联合会快报》141卷，第279 - 282页）表明谷物酶抑制剂与卡扎尔型动物蛋白酶抑制剂之间存在不同寻常的进化关系。
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