QIN Ke-Feng, HONG Mei-Xian, JIANG Chao-Zhun and MA Wen-Yu. PURIFICATION AND CHARACTERIZATION OF 30,000-DALTON STRUCTURAL PROTEIN INDUCED BY HERPES SIMPLEX VIRUS TYPE-2[J]. Virologica Sinica, 1987, 2(4).
Citation:
QIN Ke-Feng, HONG Mei-Xian, JIANG Chao-Zhun, MA Wen-Yu.
PURIFICATION AND CHARACTERIZATION OF 30,000-DALTON STRUCTURAL PROTEIN INDUCED BY HERPES SIMPLEX VIRUS TYPE-2 .VIROLOGICA SINICA, 1987, 2(4)
: 8.
单纯疱疹病毒2型3万道尔顿结构蛋白的纯化及其特性研究
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第四军医大学微生物学教研室
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第四军医大学微生物学教研室 西安
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摘要
用抗HSV-2型特异性单克隆抗体CH-A9与Sepharose 4B偶联制备免疫吸附柱,以亲和层析的方法,从HSV-2感染的BHK细胞膜上纯化了一种HSV-2特异的结构蛋白(VP30)。实验表明,该结构蛋白的主要特性有:第一,分子量为30,000道尔顿;第二,具有HSV-2型持异性;第三,可在小鼠体内诱发中和抗体。
PURIFICATION AND CHARACTERIZATION OF 30,000-DALTON STRUCTURAL PROTEIN INDUCED BY HERPES SIMPLEX VIRUS TYPE-2
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Abstract
A 30,000-dalton structural protein(VP30)on herpes simplex virus type-2 (HSV-2) -infected BHK cell membranes was purified with an immunoadsorbent column consisting of the HSV-2 type-specific monoclonal antibody(McAb) CH-A9 coupled to Sepharose 4B. The Evidence shows that the VP30 has some properties as follows: First, its molecular weight determined by sodium dodecyl sufate-polyacrylamide gel electrophoresis(SDS-PAGE)is 30,000. Second, the structural protein is HSV-2 type-specific antigen showed by indirect ...
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References
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Proportional views
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