Mochitate K, Suzuki K, Imahori K
J Biochem. 1981 May;89(5):1609-18. doi: 10.1093/oxfordjournals.jbchem.a133356.
The amino acid sequence of immunity protein (protein B) of colicin E3 (84 amino acid residues) was determined. B was first split into two fragments, CB 1 and CB 2, by CNBr treatment. The structure of CB 1 (the N-terminal part of B) was determined by Edman degradation of whole protein B. The structure of CB 2 (the C-terminal part of B) was established by sequencing its four trypsin peptides. The sequences and the alignment of the tryptic peptides were completed by analyses of thermolysin peptides of CB 2. These results established the complete amino acid sequence of B.
测定了大肠杆菌素E3免疫蛋白（蛋白B，84个氨基酸残基）的氨基酸序列。首先通过溴化氰处理将蛋白B裂解为两个片段，CB 1和CB 2。通过对整个蛋白B进行埃德曼降解确定了CB 1（蛋白B的N端部分）的结构。通过对其四个胰蛋白酶肽段进行测序确定了CB 2（蛋白B的C端部分）的结构。通过对CB 2的嗜热菌蛋白酶肽段进行分析完成了胰蛋白酶肽段的序列测定和比对。这些结果确定了蛋白B完整的氨基酸序列。
