Abstract
Phosphomonoesterases were investigated in cultivated cells infected with poliomyelitis viruses. Glycerophosphate was used as substrate with inoculated and normal samples, in parallel assays. TC fluids, homogenates and original roller tubes were used. The virus acts as an inhibitor of various enzyme systems, associating chemically or physiochemically with the enzymes in situ. During virus release or the disintegration of the host cell, this bond is ruptured and when the enzymes are of more resistant type, the original activity can be recovered. With increasing virus titers a toxic factor is developed, through virus-host interaction, which aggravates the pathological changes. The alterations of cell physiology during virus infection are illustrated by many examples. Striking enzyme changes were demonstrated in non-apparent infection with virus.

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