Kobiler D, Grosfeld H, Leitner M, Monzain R, Frist C, Seri T, Cohen S, Velan B, Shafferman A, Gozes Y
Department of Biochemistry, Israel Institute for Biological Research, Ness-Ziona.
J Interferon Res. 1989 Apr;9(2):189-93. doi: 10.1089/jir.1989.9.189.
Five murine hybridoma clones, producing monoclonal antibodies (MAbs) to bovine interferon-alpha (BoIFN-alpha) were established. One of these, F12, secreted MAbs giving high titers, in ELISA tests, neutralizing both BoIFN-alpha, -alpha C, and BoIFN-alpha D activities, belonging to the mouse IgG1 class, and having a binding affinity constant of 10(8) M-1. F12 MAbs were used for immunoaffinity purification of BoIFN-alpha, and recombinant BoIFN-alpha C from Escherichia coli extracts was purified to homogeneity in SDS-PAGE analysis and to a specific activity of 2 X 10(8) U/mg with 90% recovery of activity.
建立了五个产生针对牛α干扰素（BoIFN-α）单克隆抗体（MAb）的小鼠杂交瘤克隆。其中一个克隆F12分泌的MAb在ELISA试验中具有高滴度，能中和BoIFN-α、α C和BoIFN-α D的活性，属于小鼠IgG1类，结合亲和常数为10⁸ M⁻¹。F12 MAb用于BoIFN-α的免疫亲和纯化，从大肠杆菌提取物中纯化的重组BoIFN-α C在SDS-PAGE分析中达到了均一性，比活性为2×10⁸ U/mg，活性回收率为90%。
