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Departments of Biochemistry and Ophthalmology, University of Rochester School of Medicine and Denistry, Rochester, New York 14620
Infection of HeLa cells with herpesvirus reduced the incorporation of leucine-14C into nuclear globulins, histones, and residual protein. Infection also lowered the ratios of nuclear globulins and histones to DNA but increased the ratio of residual protein to DNA. The banding patterns in acrylamide gels of all three nuclear protein fractions were unaltered by infection. Infection did not change the relative activities of corresponding bands in all three fractions. Thus, herpes infection could not be shown to inhibit or induce the synthesis of a specific nuclear protein. The alterations in nuclear proteins appear to be the result of a general inhibition of host cell protein synthesis rather than the action of a specific protein inhibitor, such as a histone.
1 Medical Science Fellow of the Life Insurance Medical Research Fund. This work was included in a Ph.D. Thesis in biochemistry.
2 Present address: Department of Ophthalmology, McIntyre Medical Science Center, McGill University, Montreal, Quebec, Canada.
Received 3/20/69. Accepted 7/16/69.
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