Proft T, Hilbert H, Plagens H, Herrmann R
ZMBH, Mikrobiologie, Universität Heidelberg, Germany.
Gene. 1996 May 24;171(1):79-82. doi: 10.1016/0378-1119(96)00014-5.
The gene coding for the P200 protein of the bacterium, Mycoplasma pneumoniae (Mp), was cloned and sequenced. The sequence-derived data and biochemical data indicated that P200 has several features in common with the well characterized cytadherence-associated proteins, HMW1 and HMW3. These features consist of abnormal migration in SDS-PAGE, a central acidic domain with a high Pro content, repeated peptide blocks within the Pro-rich domain and P200 partitioning similar to HMW1 and HMW3 in the insoluble fraction after extraction of Mp with the detergent Triton X-100.
编码肺炎支原体(Mp)细菌P200蛋白的基因被克隆并测序。序列衍生数据和生化数据表明,P200与特征明确的细胞粘附相关蛋白HMW1和HMW3有几个共同特征。这些特征包括在SDS-PAGE中的异常迁移、富含脯氨酸的中央酸性结构域、富含脯氨酸结构域内的重复肽块以及在用去污剂Triton X-100提取Mp后,P200在不溶性部分中的分配类似于HMW1和HMW3。