Takruri I, Boulter D
Biochem J. 1979 May 1;179(2):373-8. doi: 10.1042/bj1790373.
The amino acid sequence of the ferredoxin of Triticum aestivum (wheat) was determined by using a Beckman 890C sequencer in combination with the dansyl--phenylisothiocyanate method to characterize peptides obtained by tryptic, chymotryptic and thermolytic digestion of CNBr-cleavage fragments. The molecule consists of a single polypeptide chain of 97 residues and has an unblocked N-terminus. It shows considerable similarity to other plant-type ferredoxins.
通过使用贝克曼890C测序仪结合丹磺酰 - 异硫氰酸苯酯法,对经胰蛋白酶、糜蛋白酶和热解酶消化CNBr裂解片段所得的肽段进行表征,从而确定了普通小麦铁氧化还原蛋白的氨基酸序列。该分子由一条含97个残基的单多肽链组成,且N端未封闭。它与其他植物型铁氧化还原蛋白具有相当大的相似性。