Abou-Zeid C, Harboe M, Rook G A
Department of Microbiology, School of Pathology, Middlesex Hospital Medical School, London, United Kingdom.
Infect Immun. 1987 Dec;55(12):3213-4. doi: 10.1128/iai.55.12.3213-3214.1987.
Western blot analysis showed that the 46-kilodalton (kDa) dimeric protein antigen secreted in large amounts by some daughter strains of Mycobacterium bovis BCG corresponded to protein MPB70 present in long-term culture filtrates of the Japanese substrain. The 46/23-kDa antigen is the most abundant protein in supernatant from a 5-day culture but is masked by leaked products in old culture supernatants. No similarities were found between the 46-kDa protein and MPB64, a protein with the same strain distribution, or with the antigen of similar molecular mass recognized by monoclonal antibody SA1.D2D.
蛋白质免疫印迹分析表明，卡介苗的一些子代菌株大量分泌的46千道尔顿（kDa）二聚体蛋白抗原与日本亚株长期培养滤液中存在的MPB70蛋白相对应。46/23-kDa抗原是5天培养上清液中最丰富的蛋白质，但在陈旧培养上清液中会被泄漏产物掩盖。在46-kDa蛋白与MPB64（一种具有相同菌株分布的蛋白）或与单克隆抗体SA1.D2D识别的分子量相似的抗原之间未发现相似性。
