Harrison P M, Ford G C, Smith J M, White J L
Krebs Institute for Biomolecular Research, University of Sheffield, England.
Biol Met. 1991;4(2):95-9. doi: 10.1007/BF01135385.
The nature of the amino acids whose codons border introns in ferritin genes is novel; the disposition of these intron boundaries within the three-dimensional structure of the 24-subunit molecule differs significantly from that of other proteins. These observations are discussed in relation to the functions of isoferritins.
铁蛋白基因中其密码子与内含子相邻的氨基酸的性质是新颖的;这些内含子边界在24亚基分子三维结构中的位置与其他蛋白质有显著差异。结合异铁蛋白的功能对这些观察结果进行了讨论。