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首页> 外文期刊>Polish journal of veterinary sciences >Characterization of outer membrane proteins participating in iron transport in Pasteurella multocida serotype A3.
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Characterization of outer membrane proteins participating in iron transport in Pasteurella multocida serotype A3.

机译:表征多杀巴斯德氏菌血清型A3中铁转运的外膜蛋白的特征。

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摘要

Iron-regulated outer membrane proteins (IROMPs) of P. multocida serotype A3, which function as receptors for complexes containing iron ions, are induced by iron deficiency in the bacterial growth environment. Analysis of an electrophoresis image of proteins isolated from bacteria grown on medium supplemented with 2,2'-dipyridyl revealed expression of 16 new proteins that were not noted in the case of the bacteria grown in standard conditions, with molecular weights from 30 to 160 kDa. Induction of IROMP expression occurred within 30 minutes after restricted iron conditions were established. In immunoblotting, distinct reactions were noted for proteins of molecular weight ranges of 25-49 kDa, 61-95 kDa, and 108-214 kDa. Proteins of the molecular weight of 68, 75 and 86 kDa were analysed using mass spectrometry and matched with the highest probability to proteins in the NCBI data base. Several dozen different proteins with similar amino acid sequences were matched to each sample.
机译:铁的铁调节外膜蛋白(IROMPs)。在细菌的生长环境中,铁缺乏症可诱导多杀性A3型血清型,它是含铁离子复合物的受体。对从补充有2,2'-联吡啶的培养基上生长的细菌分离出的蛋白质的电泳图谱的分析显示,在标准条件下生长的细菌中未发现16种新蛋白质的表达,分子量为30至160 kDa 。在建立限制性铁条件后的30分钟内,发生了IROMP表达的诱导。在免疫印迹中,注意到分子量范围为25-49 kDa,61-95 kDa和108-214 kDa的蛋白质发生了明显的反应。使用质谱仪分析了分子量为68、75和86 kDa的蛋白质,并与NCBI数据库中的蛋白质匹配的可能性最高。将数十个具有相似氨基酸序列的不同蛋白质与每个样品进行匹配。

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