Kingston I B, Kingston B L, Putnam F W
J Biol Chem. 1980 Apr 10;255(7):2878-85.
A histidine-rich fragment, Cp F5, with a molecular weight of 18,650 was isolated from human ceruloplasmin. It consists of 159 amino acids and contains a possible copper-binding site. The sequence of the first 18 NH2-terminal residues of Cp F5 was determined by automated Edman degradation. Cp F5 was cleaved by cyanogen bromide to produce nine fragments of from 2 to 63 residues. The amino acid sequence of all of the cyanogen bromide fragments was investigated using automated and manual Edman degradation, the fragments being digested with trypsin, chymotrypsin, thermolysin, staphylococcal protease, and pepsin as appropriate. The results, in conjunction with the data on the tryptic peptides reported in the accompanying paper (Kingston, I.B., Kingston, B.L., and Putnam, F.L. (1980) J. Biol. Chem. 255, 2886-2896), establish the complete amino acid sequence of Cp F5.
从人铜蓝蛋白中分离出一个富含组氨酸的片段Cp F5，其分子量为18,650。它由159个氨基酸组成，并含有一个可能的铜结合位点。通过自动埃德曼降解法确定了Cp F5前18个N端残基的序列。Cp F5经溴化氰裂解产生9个片段，长度从2至63个残基不等。使用自动和手动埃德曼降解法研究了所有溴化氰片段的氨基酸序列，这些片段根据需要用胰蛋白酶、胰凝乳蛋白酶、嗜热菌蛋白酶、葡萄球菌蛋白酶和胃蛋白酶进行消化。这些结果与随附论文（金斯顿，I.B.，金斯顿，B.L.，和普特南，F.L.（1980年）《生物化学杂志》255，2886 - 2896）中关于胰蛋白酶肽的数据相结合，确定了Cp F5完整的氨基酸序列。
