Suzuki M, Shimokawa H, Takagi Y, Sasaki S
Department of Biochemistry, School of Dentistry, Tokyo Medical and Dental University, Japan.
J Exp Zool. 1994 Dec 15;270(6):501-7. doi: 10.1002/jez.1402700603.
Fetuin, an abundant protein in fetal bovine plasma, is the bovine homolog of human alpha 2HS glycoprotein (alpha 2HS). In spite of numerous studies, the biological functions of both proteins remain elusive. We now report the remarkable 45Ca-binding activity of fetuin in fetal bovine serum that has been blotted on a membrane after electrophoresis. The Ca-binding ability of the purified protein was analyzed by equilibrium dialysis, which revealed that bovine fetuin had multiple Ca-binding sites, one of which had a Kd of 0.95 x 10(-4) M. It was also shown that the Ca-binding activity of fetuin was greater than that of albumin in serum of the bovine fetus at the late gestational stage. Since fetal bovine serum contains not only a high concentration of fetuin but also a high concentration of Ca, it is possible that fetuin functions to maintain high levels of Ca in fetal serum via normalization of the concentration of Ca2+ ions.
胎球蛋白是胎牛血浆中的一种丰富蛋白质,是人类α2HS糖蛋白(α2HS)的牛同源物。尽管进行了大量研究,但这两种蛋白质的生物学功能仍不清楚。我们现在报告了胎牛血清中胎球蛋白在电泳后印迹到膜上时具有显著的45Ca结合活性。通过平衡透析分析了纯化蛋白的钙结合能力,结果表明牛胎球蛋白有多个钙结合位点,其中一个的解离常数(Kd)为0.95×10⁻⁴ M。还表明,在妊娠后期牛胎儿血清中,胎球蛋白的钙结合活性大于白蛋白。由于胎牛血清不仅含有高浓度的胎球蛋白,还含有高浓度的钙,因此胎球蛋白有可能通过使Ca²⁺离子浓度正常化来维持胎儿血清中的高钙水平。