Kinetic studies on the effect of uridine diphosphate galactose and manganous ions on the reaction between lactose synthetase A protein from human milk and p-hydroxymercuribenzoate

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Abstract
The inhibition of lactose synthetase A protein by p-hydroxymercuribenzoate at pH7.5 and 25°C, which involves the reaction of one molecule of inhibitor with each molecule of enzyme, was decreased in rate by UDP-galactose, especially in the presence of Mn2+. Pseudo-first-order rate constants for the reaction between 0.1mm-p-hydroxymercuribenzoate and free enzyme, the enzyme–UDP-galactose complex and the enzyme–Mn2+–UDP-galactose complex were 4.4×10−2, 1.9×10−2 and 0.3×10−2min−1 respectively. The results also indicated that dissociation constants for UDP-galactose in the enzyme–UDP-galactose and enzyme–Mn2+–UDP-galactose complexes were 313 and 16μm respectively, the latter value being similar to the Km for UDP-galactose in the lactose synthetase reaction. The protective effect of UDP-galactose and the role of Mn2+ ions in lactose synthetase are discussed.