Takruri I, Haslett B G, Boulter D, Andrew P W, Rogers L J
Biochem J. 1978 Aug 1;173(2):459-66. doi: 10.1042/bj1730459.
The amino acid sequence of the ferrodoxin of Porphyra umbilicalis was determined by the dansyl-phenyl isothiocyanate method, on peptides obtained by tryptic, chymotryptic and thermolytic digestion of the protein or its CNBr-cleavage fragments. The molecule consists of 98 residues, has an unblocked N-terminus and shows considerable similarity with other plant-type ferredoxins. It is the first reported sequence of a red-algal ferredoxin.
采用丹磺酰基异硫氰酸苯酯法,对由蛋白质或其溴化氰裂解片段经胰蛋白酶、糜蛋白酶和嗜热菌蛋白酶消化得到的肽段进行分析,从而确定了紫菜铁氧化还原蛋白的氨基酸序列。该分子由98个残基组成,N端未封闭,与其他植物型铁氧化还原蛋白具有显著的相似性。这是首次报道的红藻铁氧化还原蛋白序列。