Litwińska B, Biesiadecka A, Gut W, Kańtoch M
National Institute of Hygiene, Department of Virology, Warszawa.
Acta Microbiol Pol. 1996;45(2):155-60.
Protein's characteristic of temperature sensitive (ts 28 degrees C) and temperature resistant (tr 39 degrees C) mutants and native HSV-1 strain was performed. Electrophoretic and Western-blott analysis of virus proteins and their reactivity tested by immunoenzymatic staining was the main subject of the presented paper. There were found no significant differences in the protein structure between native strain and its temperature clones in electrophoresis. It is important that slight differences observed in protein's antigenic reactivity of ts 28 degrees C (54 kDa) and tr 39 degrees C (99-100; 160 kDa), do not influence on the possible application of the mutants for immunization and challenging.
对蛋白质温度敏感（ts 28摄氏度）和温度抗性（tr 39摄氏度）突变体以及天然单纯疱疹病毒1型毒株的特性进行了研究。通过免疫酶染色检测病毒蛋白的电泳和蛋白质印迹分析及其反应性是本文的主要主题。在电泳中，天然毒株与其温度克隆之间的蛋白质结构未发现显著差异。重要的是，在ts 28摄氏度（54 kDa）和tr 39摄氏度（99 - 100；160 kDa）的蛋白质抗原反应性中观察到的细微差异，不会影响突变体在免疫和激发方面的可能应用。
