Affiliation:
1. Department of Microbiology, University of Mississippi School of Medicine, Jackson, Mississippi 39216
Abstract
A protein kinase which is intimately associated with equine herpesvirus (equine abortion virus) was found by using adenosine triphosphate-γ-
32
P as a phosphate donor and virus protein as an acceptor. Consistent demonstration of the activity requires prior removal of phosphohydrolase. The kinase activity requires Mg
2+
, is not stimulated by cyclic adenosine monophosphate, but is enhanced by added protamine or arginine-rich histone. The labeled product is resistant to ribonuclease, deoxyribonuclease, and chloroform-methanol but is sensitive to Pronase. Other tests suggest that serine and threonine residues are the acceptor sites. In the in vitro reaction, the incorporation represents an average of approximately 4,500 phosphate residues per virion, and all 17 virus protein bands resolved by polyacrylamide gel electrophoresis appear to be labeled.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
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5. The envelope of herpesvirus;Darlington R. W.;Progr. Med. Virol.,1969
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