Takruri I, Boulter D
Biochem J. 1980 Jan 1;185(1):239-43. doi: 10.1042/bj1850239.
The amino acid sequence of the ferredoxin of Brassica napus was determined by using a Beckman 890C sequencer in combination with the characterization of peptides obtained by tryptic and chymotryptic digestion of the protein; some peptides were subdigested with thermolysin. The molecule consists of a single polypeptide chain of 96 amino acid residues and has an unblocked N-terminus. The primary structure shows considerable similarity with other plant-type ferredoxins.
通过使用贝克曼890C测序仪,并结合对该蛋白质经胰蛋白酶和胰凝乳蛋白酶消化后所得肽段的表征,确定了甘蓝型油菜铁氧化还原蛋白的氨基酸序列;一些肽段用嗜热菌蛋白酶进行了进一步消化。该分子由一条含96个氨基酸残基的单一多肽链组成,且N端未封闭。其一级结构与其他植物型铁氧化还原蛋白有相当大的相似性。