Grov A, Flandrois J P, Fleurette J, Oeding P
Acta Pathol Microbiol Scand B. 1978 Jun;86B(3):143-7. doi: 10.1111/j.1699-0463.1978.tb00023.x.
The specific Staphylococcus aureus agglutinogen h1 has been purified and shown to be a protein with a molecular weight of about 95,000. Chemical analysis revealed all the common amino acids, except tyrosine and the sulphur-containing ones. The purified h1 antigen was strongly immunogenic in rabbits. The antiserum produced one precipitation line on double diffusion in agar against a suspension of bacteria. It also agglutinated bacteria of the h1-containing strains, as well as tanned sheep erythrocytes sensitized with h1, in high dilutions. Antibodies to other known staphylococcal antigens were not detected. The identity between h1 and Pillet's type 9 antigen was confirmed.
已纯化出特定的金黄色葡萄球菌凝集原h1,结果显示它是一种分子量约为95,000的蛋白质。化学分析表明,除酪氨酸和含硫氨基酸外,它含有所有常见氨基酸。纯化后的h1抗原在兔体内具有很强的免疫原性。该抗血清在琼脂双向扩散试验中与细菌悬液产生一条沉淀线。它还能在高稀释度下凝集含h1菌株的细菌以及用h1致敏的鞣酸处理的绵羊红细胞。未检测到针对其他已知葡萄球菌抗原的抗体。证实了h1与皮耶的9型抗原相同。