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The herpes simplex virus cx, or immediate early, protein ICP4 has been shown to be central to the control of the early stages of virus replication. The detailed mechanism of this control is unknown. In this communication we show that purified ICP4 was unable to bind to DNA even though the protein was capable of such activity in a crude extract. Addition of either infectedor uninfected-cell extracts to the purified protein restored its DNA-binding activity. These results suggest that ICP4 binds to DNA only via a component of uninfected cells.

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The initial immunization of rabbits with many protein, bacterial, and bacteriophage antigens results in the synthesis of ~,M-and 3,G-globulin hemagglutinating, agglutinating, and phage-neutralizing antibodies (1, 2). 1 On the basis of a number of observations it was suggested (1, 2) that different cells synthesize ~/M-and 3,G-globulin antibodies. ~ Further immunofluorescent studies (4, 5) of the spleens of rabbits which had been injected intravenously with diphtheria toxoid and Freund's adjuvant provided evidence for the participation of two types of cells in the synthesis of these two molecular species of antibody. Non-phagocytic mononuclear cells in the walls of the sinusoids of the red pulp contained antidiphtheria toxoid during the time when only "yM-hemagglutinating antidiphtheria toxoid was found in the serum of these animals. Later plasma cells in the non-follicular white pulp of the spleen contained antidiphtheria toxoid and the rabbits' sera had both "yM-and 3,G-globulin hemagglutinating antidiphtheria toxoid. It was, therefore, tentatively concluded that the mononuclear cells produced 3'M-globulin antitoxin and the plasma cells synthesized 7G-globulin antitoxoid.

Several structurally and functionally distinct classes of antibodies have been described for numerous species of animals. The present investigation was designed to elucidate the spectrum and interrelationships of ovine immunoglobulins (1s) and to establish the basic temporal features of the antibody response of the sheep. Materials and Methods.Purified ovine Ig were prepared by several methods from whole normal ovine serum (NOS) or immune ovine serum and from serum fractions obtained by ammonium sulfate or low ionic strength precipitation. Two stepwise elution schemes were used for the chromatographic purification of serum proteins on DEAE-cellulose. In the first, proteins were eluted by t-ris-phosphate buffer, pH 8.6, at molarities of 0.01, 0.04, 0.05, 0.08, and 0.09. In the second, proteins were eluted with 0.02, 0.035, 0.05, 0.1 and 0.15 M phosphate buffers and with 1 M NaCl, at pH 6.3. Serum was also separated by gel filtration on Sephadex G-200 using tris-HC1 buffer at pH 8 with 1 M NaCl and by preparative zone electrophoresis ( 1). Antisera to whole ovine serum and purified Ig were prepared in rabbits by the multiple injection of antigen with complete or incomplete Freund's adjuvant. Sera were rendered specific for one or more classes of Ig by stepwise absorption with appropriate ovine Ig.Microimmunoelectrophoresis (IEP) ( 2) and immunodiffusion (3) were used to characterize the antigenic relationships of Ig. Radioimmunoelectrophoresis (RIEP) (4), and passive hemagglutination (HA) (5) were used to characterize the ovine antibody response to a protein antigen, human y-globulin. Microscopic agglutination (MA) ( 6 ) ,