Richardson M
Biochem J. 1974 Jan;137(1):101-12. doi: 10.1042/bj1370101.
The amino acid sequence of subunit A of the potato chymotryptic inhibitor I was determined. The sequence was deduced from analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide, N-bromosuccinimide and dilute acid, and by digestion with trypsin, thermolysin, pepsin and papain. The molecule consists of a single polypeptide chain of 84 residues, which contains two homologous regions each of 13 amino acids. The protein does not appear to be homologous with any other known proteinase inhibitors.
已确定马铃薯胰凝乳蛋白酶抑制剂I亚基A的氨基酸序列。该序列是通过对用溴化氰、N-溴代琥珀酰亚胺和稀酸切割该蛋白质产生的片段和肽进行分析,以及用胰蛋白酶、嗜热菌蛋白酶、胃蛋白酶和木瓜蛋白酶消化后推导得出的。该分子由一条含84个残基的单一多肽链组成,其中包含两个各有13个氨基酸的同源区域。该蛋白质似乎与任何其他已知的蛋白酶抑制剂都不同源。