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pubmed-article:8385691pubmed:abstractTextA 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 10(8) 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.lld:pubmed
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pubmed-article:8385691pubmed:articleTitlePurification and properties of the herpes simplex virus type 1 UL8 protein.lld:pubmed
pubmed-article:8385691pubmed:affiliationMedical Research Council Virology Unit, Institute of Virology, Glasgow, U.K.lld:pubmed
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