Maeda K, Tsugita A, Dalzoppo D, Vilbois F, Schürmann P
Eur J Biochem. 1986 Jan 2;154(1):197-203. doi: 10.1111/j.1432-1033.1986.tb09379.x.
The complete primary structure of m-type thioredoxin from spinach chloroplasts has been sequenced by conventional sequencing including fragmentation, Edman degradation and carboxypeptidase digestion. As already reported [Tsugita, A., Maeda, K. & Schürmann, P. (1983) Biochem. Biophys. Res. Commun. 115, 1-7] these thioredoxins contain the same active-site sequence as thioredoxins from other sources. Based on the amino acid sequence thioredoxin mc contains 103 residues, has a relative molecular mass of 11425 and a molar absorption coefficient at 280 nm of 19 300 M-1 cm-1. The spinach thioredoxin mc has an overall homology of 44% with the thioredoxin from Escherichia coli mainly due to differences in the N-terminal and C-terminal regions.
通过包括片段化、埃德曼降解和羧肽酶消化在内的传统测序方法，已测定了菠菜叶绿体m型硫氧还蛋白的完整一级结构。正如之前所报道的[津田，A.，前田，K. & 舒尔曼，P.（1983年）《生物化学与生物物理研究通讯》115，1 - 7]，这些硫氧还蛋白与其他来源的硫氧还蛋白具有相同的活性位点序列。基于氨基酸序列，硫氧还蛋白mc含有103个残基，相对分子质量为11425，在280 nm处的摩尔吸收系数为19300 M⁻¹ cm⁻¹。菠菜硫氧还蛋白mc与大肠杆菌硫氧还蛋白的总体同源性为44%，主要是由于N端和C端区域存在差异。
