title: Purification and characterization of herpes simplex virus type 1 alkaline exonuclease expressed in Escherichia coli.
abstract: 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.
authors.affiliation: Infectious Diseases Section, Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.
authors.forename: J C
authors.initials: JC
authors.lastname: Bronstein
authors.forename: P C
authors.initials: PC
authors.lastname: Weber
mesh_terms: D003001:Cloning, Molecular; D004926:Escherichia coli; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D006801:Humans; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D011993:Recombinant Fusion Proteins; D012260:Ribonucleases; C066964:viral alkaline nuclease