Abstract
The activity of uridine diphosphoglucose (UDPG) dehydrogenase (UDPG: NAD + oxidoreductase, EC 1.1.1.22) from rat liver is inhibited markedly in vitro by galactosamine 1-phosphate and UDPgalactosamine. The K i value is calculated to be 6.2·10 −3 M for galactosamine-1-phosphate. The type of inhibition is non-competitive. UDPgalactosamine is effective at lower concentrations; a K i value of 6.9·10 −4 M has been measured and the inhibition is mainly competitive in nature. This inhibition of UDPG dehydrogenase activity is regarded to be responsible for the decrease of UDPglucuronate in vivo after d-galactosamine administration, supporting the significance of galactosamine 1-phosphate and UDPgalactosamine in the metabolic alterations during the development of galactosamine hepatitis.
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