Robertson J A, Stemler M E, Stemke G W
J Clin Microbiol. 1984 Feb;19(2):255-8. doi: 10.1128/jcm.19.2.255-258.1984.
All of 14 serotype standards and 34 of 35 wild-type strains of Ureaplasma urealyticum isolated from humans demonstrated an immunoglobulin A (IgA) protease activity. This activity degraded radiolabeled human IgA including IgA1 but not IgG or azocasein. The IgA fragments were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, followed by radioautography, and they had molecular weights of about 110,000 and 50,000. The IgA protease activity persisted in 25 mM EDTA but was sensitive to trypsin; it was presumed to be protein. This is the fourth microbial genus and the first myocoplasma species in which an IgA protease activity has been identified. Such activity was absent in Mycoplasma pneumoniae, Mycoplasma hominis, and Acholeplasma laidlawii.
从人类分离出的14种解脲脲原体血清型标准株及35株野生型菌株中的34株均表现出免疫球蛋白A(IgA)蛋白酶活性。该活性可降解包括IgA1在内的放射性标记的人IgA,但不降解IgG或偶氮酪蛋白。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳,随后进行放射自显影检测IgA片段,其分子量约为110,000和50,000。IgA蛋白酶活性在25 mM乙二胺四乙酸(EDTA)中持续存在,但对胰蛋白酶敏感;推测其为蛋白质。这是已鉴定出IgA蛋白酶活性的第四个微生物属,也是第一个支原体物种。肺炎支原体、人型支原体和莱氏无胆甾原体中不存在这种活性。