Coe J E, Ross M J
Biochemistry. 1987 Feb 10;26(3):704-10. doi: 10.1021/bi00377a007.
Syrian hamster female protein (SFP), a serum oligomer composed of five identical subunits, was reassociated in vitro from monomer subunits. The reconstituted pentamer was genuine by morphologic, antigenic, and structural criteria. Another female protein (FP), a homologue from Armenian hamsters (AFP), also reassociated into a pentamer after dissociation with 5 M guanidine hydrochloride. These two FP's hybridized when a mixture of them was dissociated and then reassociated. Differences between the parent FP's were used to show that the recombinant pentamer contained monomer subunits from both SFP and AFP. Reassociation of both FP's was enhanced by increasing FP concentration and also by adding Ca2+ during reassembly. The two FP's differed in their reassociation profile in that SFP was especially efficient in reassembly, whereas AFP was more dependent upon Ca2+. Female protein is a homologue of C-reactive protein and amyloid P component, and all of these proteins (pentraxins) share a similar structure. The in vitro dissociation-reassociation of female protein described herein may reflect an in vivo dissociation-reassociation which is functionally important and a common metabolic feature within this family of proteins.
叙利亚仓鼠雌性蛋白（SFP）是一种由五个相同亚基组成的血清寡聚体，它由单体亚基在体外重新缔合而成。通过形态学、抗原性和结构标准判断，重构的五聚体是真实的。另一种雌性蛋白（FP），即来自亚美尼亚仓鼠的同源物（AFP），在与5M盐酸胍解离后也重新缔合成五聚体。当将它们的混合物解离然后重新缔合时，这两种FP会发生杂交。利用亲本FP之间的差异来表明重组五聚体包含来自SFP和AFP的单体亚基。增加FP浓度以及在重新组装过程中添加Ca2+均可增强两种FP的重新缔合。两种FP在重新缔合谱方面存在差异，即SFP在重新组装方面特别高效，而AFP对Ca2+的依赖性更强。雌性蛋白是C反应蛋白和淀粉样蛋白P成分的同源物，并且所有这些蛋白（五聚素）都具有相似的结构。本文所述的雌性蛋白的体外解离 - 重新缔合可能反映了体内的解离 - 重新缔合，这在功能上很重要，并且是该蛋白家族中常见的代谢特征。
