title: Purification of the structural proteins of herpes simplex virus type 1 by reverse-phase high performance liquid chromatography.
abstract: Herpes simplex virus type-1 structural proteins were solubilized in formic acid and purified by reverse-phase high performance liquid chromatography. Purified proteins have been used to prepare monospecific polyclonal antibodies which neutralized virus infectivity in vitro.
authors.affiliation: Department of Microbiology, University of Leeds, U.K.
authors.forename: G R
authors.initials: GR
authors.lastname: Whittaker
authors.forename: D M
authors.initials: DM
authors.lastname: Meredith
mesh_terms: D000914:Antibodies, Viral / Q000276:immunology; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D009500:Neutralization Tests; D018139:Simplexvirus / Q000032:analysis* / Q000276:immunology; D015678:Viral Structural Proteins / Q000302:isolation & purification*
chemical_list: D000914:Antibodies, Viral; D015678:Viral Structural Proteins