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J Gen Virol 74 (1993), 607-612; DOI 10.1099/0022-1317-74-4-607
© 1993 Society for General Microbiology
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Purification and properties of the herpes simplex virus type 1 UL8 protein

Marc E. Parry, Nigel D. Stow and Howard S. Marsden

Medical Research Council Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, U.K.

A rapid and simple two-step scheme for the purification of herpes simplex virus type 1 UL8 protein from insect cells infected with a recombinant baculovirus has been developed. The scheme involves DEAE-Sepharose and phenyl-Sepharose chromatography and yields approximately 1.5 mg of protein from 2.4 x 108 infected cells. The protein remains intact during purification as judged by its reactivity with amino and carboxy termini-specific antisera. Gel filtration chromatography showed that the protein exists as a monomer in solution. No binding of the protein to ssDNA or dsDNA or to a DNA/RNA hybrid could be demonstrated using a gel mobility shift assay.

Received 4 August 1992; accepted 23 November 1992.


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