Aussel C, Masseyeff R
Biochem Biophys Res Commun. 1984 Mar 30;119(3):1122-7. doi: 10.1016/0006-291x(84)90891-x.
Human alpha-fetoprotein (HAFP) has three binding sites for polyunsaturated fatty acids with association constant Ka = 1.8 X 10(7) M-1. One of these binding sites overlaps with a retinoid binding site with Ka = 2.6 X 10(6)M-1. Competition experiments with bilirubin showed that this compound does not compete neither with fatty acids nor with retinoids. Thus, the two bilirubin binding sites previously demonstrated appear as two additional binding sites on HAFP. Nevertheless, the close proximity of two fatty acid binding sites and two bilirubin binding sites resulted in a modification of the binding constants for fatty acids. It is hypothesised that the binding properties of HAFP reflect the three domain structures of the protein recently deduced from the study of the nucleotide sequence of HAFP mRNA and AFPcDNA segments.
人甲胎蛋白(HAFP)有三个与多不饱和脂肪酸结合的位点,其结合常数Ka = 1.8×10⁷ M⁻¹。其中一个结合位点与一个视黄醇结合位点重叠,该视黄醇结合位点的Ka = 2.6×10⁶ M⁻¹。用胆红素进行的竞争实验表明,该化合物既不与脂肪酸竞争,也不与视黄醇竞争。因此,先前证明的两个胆红素结合位点似乎是HAFP上另外两个结合位点。然而,两个脂肪酸结合位点和两个胆红素结合位点的紧密相邻导致了脂肪酸结合常数的改变。据推测,HAFP的结合特性反映了最近通过对HAFP mRNA和AFPcDNA片段核苷酸序列研究推导出来的该蛋白质的三结构域结构。