An immobilized native bovine enzyme is used to release a drug from its
recombinant construct. The drug is then passed through a 5,000 MW
cellulose triacetate membrane (the drug could be mixed with a 10,000
dalton fluorophore as a QC/QA test of the membrane integrity, prions
having >23kD molecular weight). Would this solve the problem of
requiring the immobilized native bovine enzyme to be absolutely free of
TSEs(multiple ultrafiltration membranes could be used for added
insurance)? The reason for even asking this question is that "native
bovine enzyme" is not only much less expensive than the recombinant
form, but is also enzymatically superior.