Akerström B, Nilsson K, Berggård B, Berggård I
J Immunol. 1979 Jun;122(6):2516-20.
alpha 1-Microglobulin was found by immunofluorescence not to be associated with human lymphoid and nonlymphoid cell lines. No accumulation of alpha 1-microglobulin was detected in culture media of these cell lines. A weak membrane fluorescence with anti-alpha 1-microglobulin on peripheral lymphocytes could not be blocked by the purified protein. No release of alpha 1-microglobulin into the growth medium was seen by normal cultured leukocytes. Treatment of normal lymphocytes, erythrocytes, and various cell lines with solubilization techniques did not yield any alpha 1-microglobulin. alpha 1-Microglobulin and protein HC display immunologic and biochemical identity. However, anti-protein HC stained almost all of the tested cell lines and normal lymphocytes. Blocking experiments with the purified protein were not successful. Antibodies reacting with a minor impurity (50,000 d) in the alpha 1-microglobulin or protein HC preparations could be absorbed from anti-alpha 1-microglobulin with normal leukocytes and a lymphoid cell line.
通过免疫荧光法发现α1-微球蛋白与人类淋巴细胞系和非淋巴细胞系无关。在这些细胞系的培养基中未检测到α1-微球蛋白的积累。外周淋巴细胞上抗α1-微球蛋白的微弱膜荧光不能被纯化蛋白阻断。正常培养的白细胞未见α1-微球蛋白释放到生长培养基中。用增溶技术处理正常淋巴细胞、红细胞和各种细胞系未产生任何α1-微球蛋白。α1-微球蛋白和蛋白HC在免疫学和生物化学特性上一致。然而,抗蛋白HC几乎能使所有测试的细胞系和正常淋巴细胞染色。用纯化蛋白进行的阻断实验未成功。与α1-微球蛋白或蛋白HC制剂中的一种次要杂质(50,000道尔顿)反应的抗体可被正常白细胞和一种淋巴细胞系从抗α1-微球蛋白中吸收。