Journal article
Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1.
Abstract
A glutathione S-transferase fusion to the COOH-terminal acidic transactivation domain of Vmw65 from herpes simplex virus type 1 was overexpressed in Escherichia coli and isolated by affinity chromatography on glutathione-Sepharose. Following cleavage of the fusion protein with thrombin, the transactivation domain was purified to homogeneity by ion exchange chromatography yielding approximately 0.6 mg of protein/liter of bacterial culture. …
Authors
Donaldson L; Capone JP
Journal
Journal of Biological Chemistry, Vol. 267, No. 3, pp. 1411–1414
Publisher
Elsevier
Publication Date
1 1992
DOI
10.1016/s0021-9258(18)45957-1
ISSN
0021-9258