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首页> 外文期刊>Journal of Virology >Late nonstructural 100,000- and 33,000-dalton proteins of adenovirus type 2. II. Immunological and protein chemical analysis.
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Late nonstructural 100,000- and 33,000-dalton proteins of adenovirus type 2. II. Immunological and protein chemical analysis.

机译:腺病毒型22型的晚期非结构100,000-和33,000dalton蛋白。免疫和蛋白质化学分析。

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摘要

For an immunological analysis of the late adenovirus type 2 nonstructural 100,000-dalton (100K) and 33K proteins, we prepared antisera against sodium dodecyl sulfate-denatured, gel-purified 100K and 33K proteins. These antisera were tested for potential cross-reactivity, since according to a previous report (Axelrod, Virology 87:366--383, 1978) these two proteins exhibit extensive amino acid homologies. However, immunoprecipitations of 100K and 33K proteins, as well as a sensitive immune replica technique, did not reveal any immunological relationship between these proteins. Therefore, using fingerprint peptide analysis, we investigated the structural relationship between 100K and 33K proteins labeled with a 14C-amino acid mixture or with [14C]proline after digestion with trypsin. We detected only minor, if any, amino acid homologies, indicating that the 100K and 33K proteins are not structurally related.
机译:对于晚期腺病毒2型非结构100,000-DALTON(100K)和33K蛋白的免疫学分析,我们将抗血清对十二烷基硫酸钠 - 变性,凝胶纯化的100K和33K蛋白制备。这些抗血清被测潜在的交叉反应性,因为根据先前的报告(Axelrod,病毒学87:366-383,1978),这两种蛋白质表现出广泛的氨基酸同源物。然而,100K和33K蛋白的免疫沉淀以及敏感的免疫复制品技术没有揭示这些蛋白质之间的任何免疫关系。因此,使用指纹肽分析,我们研究了用胰蛋白酶消化后用14℃氨基酸混合物或用[14C]脯氨酸标记的100k和33k蛋白之间的结构关系。我们仅检测到次要的氨基酸同源物,表明100K和33K蛋白质没有结构相关。

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