Saada A B, Terespolski Y, Adoni A, Kahane I
Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Infect Immun. 1991 Jan;59(1):467-9. doi: 10.1128/iai.59.1.467-469.1991.
Ureaplasma urealyticum (four serotypes and two clinical isolates) were metabolically labeled with radioactive methionine to a high specific activity. Labeling allowed the study of the mechanism of adherence to human erythrocytes. The adherence mechanism was complex and partially mediated by proteinaceous surface components. The binding sites on the erythrocytes were partially sensitive to neuraminidase treatment, and adherence was inhibited by glycophorin and dextran sulfate, indicating recognition of sialyl residues and sulfated compounds.
解脲脲原体(四种血清型和两种临床分离株)用放射性甲硫氨酸进行代谢标记,以达到高比活性。标记有助于研究其与人红细胞的黏附机制。黏附机制复杂,部分由蛋白质表面成分介导。红细胞上的结合位点对神经氨酸酶处理部分敏感,糖蛋白和硫酸葡聚糖可抑制黏附,表明其识别唾液酸残基和硫酸化化合物。