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一种具有免疫显性的90千道尔顿烟曲霉抗原是过氧化氢酶的亚基。

An immunodominant 90-kilodalton Aspergillus fumigatus antigen is the subunit of a catalase.

作者信息

López-Medrano R, Ovejero M C, Calera J A, Puente P, Leal F

机构信息

Departamento de Microbiología y Genética, Universidad de Salamanca, Consejo Superior de Investigaciones Científica, Spain.

出版信息

Infect Immun. 1995 Dec;63(12):4774-80. doi: 10.1128/iai.63.12.4774-4780.1995.

Abstract

We have identified, purified, and characterized structurally and functionally a 90-kDa immunodominant antigen associated with the water-soluble fraction of Aspergillus fumigatus. This antigen is recognized by 90.3% of serum samples from patients with aspergilloma and should be considered either by itself or better in combination with other purified antigens as a candidate for developing a standardized immunoassay for the detection of aspergilloma. p90 is a glycoprotein containing at least two two N-linked sugar chains of 2 and 5 kDa, respectively, which are not necessary for its reactivity with aspergilloma serum samples. Using specific anti-p90 rabbit serum, we have demonstrated that under native conditions, p90 exists in oligomeric form and has associated catalase activity. This activity is resistant to extreme temperatures (> 60 degrees C), reducing agents (40 mM dithiothreitol), high concentrations of denaturing agents such as 8 M urea and 8% sodium dodecyl sulfate, and treatments with ethanol-chloroform-water (5:3:10 [vol/vol]) mixtures.

摘要

我们已经鉴定、纯化并在结构和功能上表征了一种与烟曲霉水溶性部分相关的90 kDa免疫显性抗原。90.3%的曲菌球患者血清样本可识别该抗原,应单独或更好地与其他纯化抗原结合考虑,将其作为开发用于检测曲菌球的标准化免疫测定的候选物。p90是一种糖蛋白,分别含有至少两条2 kDa和5 kDa的N-连接糖链,这些糖链对于其与曲菌球血清样本的反应性并非必需。使用特异性抗p90兔血清,我们已经证明在天然条件下,p90以寡聚体形式存在并具有相关的过氧化氢酶活性。该活性对极端温度(>60摄氏度)、还原剂(40 mM二硫苏糖醇)、高浓度变性剂如8 M尿素和8%十二烷基硫酸钠以及用乙醇-氯仿-水(5:3:10 [体积/体积])混合物处理具有抗性。

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本文引用的文献

1
An 88-kilodalton antigen secreted by Aspergillus fumigatus.烟曲霉分泌的一种88千道尔顿抗原。
Infect Immun. 1993 Nov;61(11):4767-71. doi: 10.1128/iai.61.11.4767-4771.1993.
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Aspergillus fumigatus antigens.烟曲霉抗原
Microbiology (Reading). 1995 Oct;141 ( Pt 10):2699-704. doi: 10.1099/13500872-141-10-2699.
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Effect of deglycosylation on the stability of Aspergillus niger catalase.
Arch Biochem Biophys. 1981 Dec;212(2):385-92. doi: 10.1016/0003-9861(81)90379-9.

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