Isolation by high-performance liquid chromatography and partial characterization of a 57,000-dalton herpes simplex virus type 1 polypeptide.
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.
Welling-Wester
S
S
Popken-Boer
T
T
Wilterdink
J B
JB
van Beeumen
J
J
Welling
G W
GW
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
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D010455:Peptides; D014764:Viral Proteins; D015678:Viral Structural Proteins