Studies on protein and nucleic acid metabolism in virus-infected mammalian cells. 2. The isolation, crystallization and chemical characterization of mouse encephalomyocarditis virus

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Abstract
A method for large-scale production of encephalomyocarditis virus has been developed. The behavior of the virus on columns of diethylaminoethylcellulose, ECTEOLA-cellulose and calcium phosphate has been studied. Crystalline virus has been obtained from effluents after chromatography on calcium phosphate columns. The virus has been shown to be a ribonucleoprotein containing about 30% of ribonucleic acid. Electron-microscope photographs show that the virus is a spheroid with a diameter of about 27 m[mu] (dry). Particle counts indicate that about 10% of the particles in a crystalline preparation are infective (as shown by plaque counts). This compares very favourably with crystalline preparations of poliomyelitis virus. The base composition of the viral ribonucleic acid has been determined and also the amino acid composition of the viral protein. Virus hemagglutinin is associated with and is purified along with the virus. It is concluded that the hemagglutinin is the virus protein.