Ripalti A, Landini M P, La Placa M
Institute of Microbiology, University of Bologna, Medical Faculty, Italy.
Microbiologica. 1988 Jan;11(1):69-76.
DNase activity can be detected in lysates of extensively purified human cytomegalovirus (HCMV) particles. The presence of activity only in purified virions and not in dense bodies and its neutralization by HCMV-positive human sera strongly suggest that the enzyme is virus-specific. In situ analysis of the enzymatic activity of individual HCMV polypeptides, separated in a DNA-containing polyacrylamide gel, has shown that the DNase activity present in purified virions is mainly associated with a polypeptide of 46,000 dalton MW (p46). A monospecific anti-p46 serum, raised in mice, neutralizes about 80% of the DNase activity present in extracts of purified virions and recognizes an enzymatically inactive, 76,000 dalton MW polypeptide both in non-infected and HCMV-infected cells.
在广泛纯化的人巨细胞病毒（HCMV）颗粒的裂解物中可检测到脱氧核糖核酸酶（DNase）活性。仅在纯化的病毒粒子中存在该活性，而在致密体中不存在，并且其被HCMV阳性人血清中和，这强烈表明该酶是病毒特异性的。对在含DNA的聚丙烯酰胺凝胶中分离的单个HCMV多肽的酶活性进行原位分析表明，纯化病毒粒子中存在的DNase活性主要与分子量为46,000道尔顿（p46）的多肽相关。在小鼠中产生的单特异性抗p46血清可中和纯化病毒粒子提取物中约80%的DNase活性，并在未感染和HCMV感染的细胞中识别出一种无酶活性、分子量为76,000道尔顿的多肽。
