Nishi S, Matsue H, Yoshida H, Yamaoto R, Sakai M
Department of Biochemistry, Hokkaido University School of Medicine, Sapporo, Japan.
Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3102-5. doi: 10.1073/pnas.88.8.3102.
Rat alpha-fetoprotein (AFP) has been demonstrated to bind estrogen, whereas human AFP lacks the activity. We constructed four chimeric molecules from cDNAs encoding these AFPs with the use of two restriction sites common to them and expressed them as well as rat and human AFP cDNA in yeast. The recombinant molecules were purified, characterized, and found to have the predicted structures. Analyses of estrogen binding indicated that a rat AFP sequence composed of residues 423-506 that contains 31 rat-specific amino acids is essential for the activity.
已证明大鼠甲胎蛋白（AFP）能结合雌激素，而人类AFP则缺乏这种活性。我们利用编码这些AFP的cDNA构建了四个嵌合分子，使用它们共有的两个限制性酶切位点，并在酵母中表达这些嵌合分子以及大鼠和人类AFP cDNA。对重组分子进行了纯化、表征，发现其具有预测的结构。雌激素结合分析表明，由423 - 506位残基组成的大鼠AFP序列（包含31个大鼠特有的氨基酸）对该活性至关重要。
