Maita T, Matsuda G
Hoppe Seylers Z Physiol Chem. 1980;361(2):105-17. doi: 10.1515/bchm2.1980.361.1.105.
The carboxymethylated L-asparaginase from Escherichia coli A-1--3 was fragmented with cyanogen bromide and the resulting peptides were isolated by using gel filtration on Sephadex G-50 and column chromatography on DE-52. The amino acid sequences of the 7 cyanogen bromide peptides thus obtained were established completely or partially by further fragmentation with trypsin, chymotrypsin and pepsin, and the Dansyl Edman method. Based on the above results and the complete sequences of the tryptic peptides from the carboxymethylated L-asparaginase reported in the previous paper, the whole sequence of the enzyme was established. The reported sequence consists of 321 amino acid residues and its calculated molecular weight is 34 080.
来自大肠杆菌A-1--3的羧甲基化L-天冬酰胺酶用溴化氰裂解，所得肽段通过在Sephadex G-50上进行凝胶过滤和在DE-52上进行柱色谱分离。通过用胰蛋白酶、胰凝乳蛋白酶和胃蛋白酶进一步裂解以及丹磺酰-埃德曼法，完全或部分确定了由此获得的7个溴化氰肽段的氨基酸序列。基于上述结果以及前一篇论文中报道的羧甲基化L-天冬酰胺酶胰蛋白酶肽段的完整序列，确定了该酶的完整序列。报道的序列由321个氨基酸残基组成，其计算分子量为34080。
