In:
Journal of Virology, American Society for Microbiology, Vol. 54, No. 2 ( 1985-05), p. 265-270
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.
Type of Medium:
Online Resource
ISSN:
0022-538X
,
1098-5514
DOI:
10.1128/jvi.54.2.265-270.1985
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
1985
detail.hit.zdb_id:
1495529-5
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