豚鼠细胞表面白喉毒素结合糖蛋白的免疫沉淀及部分特性分析
Immunoprecipitation and partial characterization of diphtheria toxin-binding glycoproteins from surface of guinea pig cells.
作者信息
Proia R L, Hart D A, Holmes R K, Holmes K V, Eidels L
出版信息
Proc Natl Acad Sci U S A. 1979 Feb;76(2):685-9. doi: 10.1073/pnas.76.2.685.
Abstract
125I-Labeled membrane glycoproteins that specifically interact with diphtheria toxin and CRM197 protein--but not with diphtheria toxoid, fragment A of diphtheria toxin, or cholera toxin--were detected by use of the lactoperoxidase labeling technique followed by an immunoprecipitation system. These glycoproteins, which adhere to lentil lectin-Sepharose columns, are present on the surface of diphtheria toxin-sensitive guinea pig lymph node cells but are completely lacking on the surface of diphtheria toxin-resistant mouse L cells. The major 125I-labeled glycoprotein that interacts with diphtheria toxin exhibits anomalous behavior, characteristic of glycoproteins, when analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. This demonstration of the biochemical nature of specific diphtheria toxin binding membrane components raises the possibility that the detected components are diphtheria toxin receptors.
摘要
利用乳过氧化物酶标记技术，随后通过免疫沉淀系统，检测到了125I标记的膜糖蛋白，这些膜糖蛋白能与白喉毒素和CRM197蛋白特异性相互作用，但不与白喉类毒素、白喉毒素A片段或霍乱毒素相互作用。这些附着在扁豆凝集素-琼脂糖柱上的糖蛋白存在于对白喉毒素敏感的豚鼠淋巴结细胞表面，但在对白喉毒素有抗性的小鼠L细胞表面则完全缺失。通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳分析时，与白喉毒素相互作用的主要125I标记糖蛋白表现出糖蛋白特有的异常行为。对白喉毒素特异性结合膜成分的生化性质的这一证明增加了所检测到的成分是白喉毒素受体的可能性。
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