Abstract

1. 1. Several enzymes of the glucuronic acid pathway were studied in the 7200–12,800 g fraction isolated from the digestive gland of the blue crab. 2. 2. UDPglucose dehydrogenase was observed to reduce NAD when UDPG was the substrate. UDPglucuronic acid acted as substrate for both UDPGApyrophosphatase and UDPGAglucuronyltransferase. EDTA inhibited UDPGA-pyrophosphatase which resulted in increased glucuronide formation. Alkaline phosphatase activity was linear with respect to increased concentration of p- nitrophenyl-β- d- glucuronide . Saccharo-1,4-lactone was observed to have a g great inhibitory effect upon β-glucuronidase. 3. 3. More substrate appears to be utilized via the UDPGA→GA-1-P→GA than UDPGA→glucoronide→GA sequence of reactions because pyrophosphatase activity is greater than transferase activity. 4. 4. It appears, therefore, that the UDPglucose to glucuronic acid part of the glucuronic acid pathway in the blue crab is similar to that reported in mammals.

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