Bronstein J C, Weber P C
Infectious Diseases Section, Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.
J Virol. 1996 Mar;70(3):2008-13. doi: 10.1128/JVI.70.3.2008-2013.1996.
The alkaline exonuclease (AE) encoded by the herpes simplex virus type 1 (HSV-1) UL12 open reading frame was inducibly expressed in Escherichia coli and purified without the use of chromatographic separation. This recombinant AE was found to exhibit the same biochemical properties as the virus-encoded protein and was used to confirm the existence of a weak endonucleolytic activity in the enzyme. Antisera raised against the recombinant protein recognized several forms of the AE in HSV-1-infected cells. This expression and purification strategy will provide an economical and easily accessible alternative source of HSV-1 AE for future in vitro studies.
由单纯疱疹病毒1型（HSV-1）UL12开放阅读框编码的碱性核酸外切酶（AE）在大肠杆菌中可诱导表达，且无需色谱分离即可纯化。发现这种重组AE具有与病毒编码蛋白相同的生化特性，并用于证实该酶中存在微弱的核酸内切酶活性。针对重组蛋白产生的抗血清识别HSV-1感染细胞中的几种AE形式。这种表达和纯化策略将为未来的体外研究提供一种经济且易于获取的HSV-1 AE替代来源。
