Protein characterization ofBabesia equi piroplasms isolated from infected horse erythrocytes
Protein characterization ofBabesia equi piroplasms isolated from infected horse erythrocytes
复制标题
从受感染的马红细胞中分离出的马巴贝斯虫梨原体的蛋白质特征
DOI:
10.1007/bf00932505
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发表时间:
2004
影响因子:
2
通讯作者:
M. Kamada
中科院分区:
文献类型:
--
作者:
S. Ali;C. Sugimoto;M. Matsuda;T. Sugiura;T. Kanemaru;M. Onuma;M. Kamada
Proteins ofBabesia equipiroplasms were characterized. The piroplasms ofB. equiwere purified by lysis of infected horse erythrocytes with N2gas cavitation followed by separation in Percoll density-gradient centrifugation. The relative molecular weights (Mr) of major proteins separated by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis were 18, 28, 30, 41, 43, 54, 66.5, and 96 kDa. Immunoblot analysis using serum from an experimentally infected horse revealed six immunodominant proteins of 15, 18, 28, 30, 41, and 96 kDa. Two immunodominant proteins of 18 and 28 kDa were membrane-bound proteins as revealed by Triton X-114 phase partitioning.