Medow I, Rüsch-Gerdes S, Schröder K H
Forschungsinstitut Borstel, Federal Republic of Germany.
Zentralbl Bakteriol Mikrobiol Hyg A. 1987 Oct;266(3-4):359-69. doi: 10.1016/s0176-6724(87)80216-x.
Ribosomal proteins from Mycobacterium tuberculosis H37 Rv were analyzed by polyacrylamide gel electrophoresis and 73 proteins were separated. The 30S subunit consists of 26 proteins, the 50S subunit of 41 proteins, 6 proteins of the ribosomes could not be shown in the subunits. The molecular weights for the proteins of the 30S subunit are 9100-43500, and for the proteins of the 50S subunit 8000-46000. The sedimentation coefficient have values of 28.8S and 47.7S. It was demonstrated that streptomycin-resistant cells in comparison to sensitive cells have two additional 30S proteins. Moreover, the protein L34 has changed its position. Kanamycin- and capreomycin-resistant cells have also two additional proteins, but viomycin shows no changes.
对结核分枝杆菌H37 Rv的核糖体蛋白进行了聚丙烯酰胺凝胶电泳分析,分离出73种蛋白质。30S亚基由26种蛋白质组成,50S亚基由41种蛋白质组成,核糖体的6种蛋白质在亚基中未显示。30S亚基蛋白质的分子量为9100 - 43500,50S亚基蛋白质的分子量为8000 - 46000。沉降系数分别为28.8S和47.7S。结果表明,与敏感细胞相比,链霉素抗性细胞有两种额外的30S蛋白质。此外,蛋白质L34的位置发生了变化。卡那霉素和卷曲霉素抗性细胞也有两种额外的蛋白质,但紫霉素没有变化。