胰岛素的B链羧端八肽与胰岛素分子的活性有密切关系。根据布罗默(Bromer)和钱斯(Chance)的报道,胰岛素用胰蛋白酶水解去掉B链羧端八肽后,剩下的四十三肽只具有原胰岛素活力的1％左右。但是,在羧端八肽中并非所有的氨基酸都是胰岛素表现活力所必须的。根据哈里斯(Harris)和李(Li)的报道,去除胰岛素B链羧端的丙氨酸并 Insulin B chain carboxy terminal octapeptide is closely related to the activity of insulin molecules. According to reports by Bromer and Chance, after insulin is removed by trypsin hydrolysis of the B-chain carboxy-terminal octapeptide, the remaining forty-three peptide has only about 1% of the original insulin activity. However, not all amino acids in the carboxy-terminal octapeptide are necessary for insulin to exert its activity. According to reports by Harris and Li, alanine at the carboxy-terminal end of the insulin B chain is removed