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A mycovirus has been purified from mycelia of Penicillium chrysogenum by isopycnic centrifugation in sucrose and in CsCl. Viral particles band with a buoyant density of 1.20 in sucrose and 1.38 in CsCl. Particles have icosohedral symmetry, are 35 nm in diameter, and have an absorption profile characteristic of nucleoprotein. One enzymatic activity, RNA polymerase, is associated with the purified mycophage. Nucleic acid extracted from purified virus has a buoyant density in CS2SO4 of 1.61, a molar extinction coefficient of εp (258 nm) of 7200, a s20, w of 13.0, and a pattern of circular dichroism characteristic of double-helical ribonucleic acid. Molecules of this double-stranded ribonucleic acid (dsRNA), examined by electron microscopy, have a mean contour length of 0.86 μm which corresponds to a molecular weight of about 2.0 × 106 daltons. This dsRNA is resolved further by acrylamide gel electrophoresis into three closely spaced bands. Thermal denaturation of the viral dsRNA is dependent on ionic strength and gives a linear relationship with the negative logarithm of the sodium ion concentration.

The final step in the biosynthesis of mycophenolic acid involves the transfer of a methyl group from S -adenosylmethionine to demethylmycophenolic acid. The enzyme, S -adenosylmethionine:demethylmycophenolic acid O -methyltransferase, was isolated from Penicillium stoloniferum and purified 2,700-fold by ammonium sulfate fractionation and diethylaminoethyl-cellulose and Sephadex G-200 chromatography. Maximum enzyme activity was achieved at pH 7.5 and a temperature of 27 to 28 C. The apparent K m for demethylmycophenolic acid was 3.1 × 10 −6 M. The enzyme preparation was 50% inactivated when exposed to 33 C for 15 min. Mycophenolic acid, homocystine, S -adenosyl-homocysteine, ethanol, and Mg 2+ inhibited the methyltransferase. This enzyme appears to be subject to end product inhibition which may regulate the synthesis of mycophenolic acid. The methyltransferase activity was highest during the early phases of the fermentation.

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