cell protease complexes cancer cells produce peptides which are homologous to the enzyme binding sites of u221d 1 pi these peptides are capable of binding with proteases in a manner whereby u221d 1 pi and protease binding is prevented but still permits the formation of cancer cell protease complexing the effectiveness of the peptide binding with the serine proteases has profound affect on the intracellular events by unbalancing normal control mechanisms and key switches in the cascade of irreversible biochemical processes as a result there is a switching off of the production of u221d 1 pi and reduction in the controls to prevent cancer cell proliferation consequently any proteolytic process regulation by inhibition control involved in the derepression of genes e g those coding for biologically active proteins and those coding concomitantly for the cancer associated proteases and their regulatory u221d 1 pi inhibitor along with the synthesis of cancer cell peptides would in turn retain their proteolytic activity by the formation of the protease peptide complexes instead of normal enzyme u221d 1 pi complexes it has now been found that the balance can be restored by the administration of u221d 1 pi alone or in combination with other serine protease inhibitors and or alpha 2 macroglobulin in an amount and for a time that proteolytic activity of protease inhibitors produced by the liver is sufficient in the case of virally produced cancer cells u221d 1 pi has been found.