title: Isolation by high-performance liquid chromatography and partial characterization of a 57,000-dalton herpes simplex virus type 1 polypeptide.
abstract: A Nonidet P-40 extract of HSV-1-purified virions was fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC). The first peak fraction eluted at 25% organic solvent. Polyacrylamide gel electrophoresis showed that it contained a 57,000-dalton polypeptide. The polypeptide was characterized by determination of the amino acid composition and the N-terminal amino acid sequence. Adsorption of the detergent extract before RP-HPLC showed that the polypeptide reacted with monoclonal antibodies LP1 directed against herpes simplex virus polypeptide VP-16.
authors.forename: S
authors.initials: S
authors.lastname: Welling-Wester
authors.forename: T
authors.initials: T
authors.lastname: Popken-Boer
authors.forename: J B
authors.initials: JB
authors.lastname: Wilterdink
authors.forename: J
authors.initials: J
authors.lastname: van Beeumen
authors.forename: G W
authors.initials: GW
authors.lastname: Welling
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal / Q000276:immunology; D002851:Chromatography, High Pressure Liquid; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis*; D018139:Simplexvirus / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis* / Q000276:immunology; D015678:Viral Structural Proteins
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D010455:Peptides; D014764:Viral Proteins; D015678:Viral Structural Proteins