Abstract
Summary
In separating the various effects of neomycin sulfate which may be exerted in systems designed to measure the activity of lipase, it is apparent that the antibiotic enhances the activity of both porcine and human lipase on an insoluble substrate. Additionally, it has the propensity to unstabilize emulsions. These effects are antagonistic and may account for divergent results previously recorded regarding neomycin-lipase interrelationships. Both the enzyme enchancing and emulsion unstabilizing properties of the antibiotic seem to reside in the presence of its free amino groups.
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