磷脂酶A2活性与单纯疱疹病毒特异性Fc受体蛋白一起被共纯化。
Phospholipase A2 activity is copurified together with herpes simplex virus-specified Fc receptor proteins.
作者信息
Lehtinen M, Koivisto V, Lahtinen P, Lehtinen T, Aaran R K, Leinikki P
机构信息
Institute of Biomedical Sciences, University of Tampere, Finland.
出版信息
Intervirology. 1988;29(1):50-6. doi: 10.1159/000150028.
We purified Fc-binding proteins from herpes simplex virus (HSV)-infected Vero cells by using an inverse immunoaffinity column chromatography. Polyacrylamide gel electrophoresis analysis revealed a single, virus-specific 65-kd polypeptide both in HSV type 1- and HSV type 2-infected cell-derived preparations. A Ca2+-dependent phospholipase A2 activity was demonstrated to be associated with the viral Fc-binding proteins.
我们通过使用反向免疫亲和柱色谱法从单纯疱疹病毒（HSV）感染的非洲绿猴肾细胞（Vero细胞）中纯化出Fc结合蛋白。聚丙烯酰胺凝胶电泳分析显示，在1型和2型HSV感染细胞来源的制剂中均存在一条单一的、病毒特异性的65-kd多肽。已证明一种Ca2+依赖性磷脂酶A2活性与病毒Fc结合蛋白相关。
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