Wiker H G, Harboe M, Nagai S, Patarroyo M E, Ramirez C, Cruz N
Int Arch Allergy Appl Immunol. 1986;81(4):307-14. doi: 10.1159/000234154.
The MPB59 protein of Mycobacterium bovis BCG was purified to homogeneity from culture fluid of BCG substrain Tokyo, and characterized by biochemical and immunological techniques. The molecular weight was 28,000, determined by SDS-polyacrylamide gel electrophoresis, and the pI value was 5.3. The N-terminal amino acid sequence was determined for 32 steps and showed no significant homology with MPB64, MPB70 or MPB80. By crossed immunoelectrophoresis, MPB59 was found to belong to the BCG antigen 85 complex and identified as corresponding to the 85B component of this complex. The protein cross-reacted extensively with other species of mycobacteria, and induced a marked humoral immune response in armadillos and monkeys during development of systemic mycobacterial infection after inoculation with Mycobacterium leprae.
从卡介苗东京亚株的培养液中纯化出牛分枝杆菌卡介苗的MPB59蛋白，并使其达到均一性，然后采用生化和免疫技术对其进行表征。通过SDS-聚丙烯酰胺凝胶电泳测定其分子量为28,000，pI值为5.3。测定了其N端32个氨基酸序列，结果显示与MPB64、MPB70或MPB80无明显同源性。通过交叉免疫电泳发现，MPB59属于卡介苗抗原85复合物，并被鉴定为对应于该复合物的85B组分。该蛋白与其他分枝杆菌种类广泛交叉反应，并在接种麻风分枝杆菌后全身性分枝杆菌感染的发展过程中，在犰狳和猴子体内诱导出显著的体液免疫反应。
