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纤维结合蛋白(fibronectin,Fn)是近15年中被人们重视的一种蛋白质。早在1948年Morrison等发现,血液在低温条件下有一种与纤维蛋白原组分相仿,但又不同于纤维蛋白原的蛋白质析出,称为冷非溶性球蛋白。1957年Smith等发现,正常人或病人的血浆中,加肝素后,在较低温度下,都可获得该冷沉淀物。直到1970年Mosesson等才分离和提纯了这种蛋白质。近十余年,国外许多学者对这一种蛋白质的结构、性质、生物学活性和临床意义进行了大量的研究,认为它是一种多功能的蛋白质,对它的命名不下十余种。目前,倾向用纤维结合蛋白的名称。一、Fn的生化性质和分子结构Rennard等通过鼠-人细胞杂交试验,应用特异的酶免疫法定位研究,进一步证实
Fibronectin (Fn) is a protein that has been valued in recent 15 years. As early as 1948, Morrison et al. Found that at low temperatures, blood has a protein that is similar to fibrinogen but different from fibrinogen, called cold non-soluble globulin. In 1957, Smith et al. Found that cold deposits were obtained at lower temperatures in both normal and patient plasma following addition of heparin. It was not until about 1970 that Mosesson et al. Isolated and purified this protein. In the past ten years or so, many foreign scholars have done a lot of research on the structure, properties, biological activity and clinical significance of this protein. They think it is a multi-functional protein, and its name is no less than ten species. Currently, the name of fibronectin is favored. First, the biochemical properties of Fn and molecular structure Rennard through mouse-human cell hybridization test, the application of specific enzyme immunoassay localization study, further confirmed