Abstract

The presence of nonspecific UDP-galactose hydrolases in mammary tissue homogenates interferes with the radioactive assays of the A and B components of lactose synthetase. Uridine triphosphate was added to assay incubation mixtures and was found to effectively inhibit the hydrolase activity with a minimal influence on the specific A and B protein activities. This effect was present over a wide range of mammary tissue homogenate protein concentrations and incubation times. It is suggested that this modification will improve the specificity of existing radioactive assays of lactose synthetase.

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