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首页> 外文期刊>The Korean Journal of Parasitology >Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation
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Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation

机译：曼氏螺旋藻蝶藻中31 kDa分子的酶N-聚糖分析及其化学氧化后的抗原性

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摘要

A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electropheretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-gly-cosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.
机译：通过明胶亲和力和Mono Q阴离子交换柱色谱法获得了曼氏螺旋藻（sparganum）的蝶形猴的31 kDa的高特异性抗原蛋白。将纯化的31 kDa蛋白进行N-聚糖酶消化以进行结构分析。在消化之前和之后，通过SDS-PAGE分析相对电迁移率。在酶消化后的SDS-PAGE上，31 kDa的蛋白质显示出大约2 kDa的分子位移，这表明拥有复杂的N-连接的寡糖（对N-糖苷-糖苷酶F敏感），但不具有高甘露糖寡糖（内切- β-N-乙酰氨基葡糖苷酶H，不敏感）。通过酶联免疫吸附测定（ELISA），化学终止的31 kDa蛋白与人的脊柱侧凸血清相比在统计学上无显着变化。因此，发现在人鞘菌中31kDa分子的主要表位主要是多肽，而在石笋中的抗原性分子的N-聚糖在抗碳水化合物抗体的产生中最少。

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