Glucuronidation in the reindeer: dietary modification in the UDP-glucuronosyltransferase activity with 4-nitrophenol, 1-naphthol and phenolphthalein as acceptors |
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| Authors: | R Juvonen M Laitinen E Hietanen M Nieminen |
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| Affiliation: | 1. School of Agricultural Computational and Environmental Sciences, International Centre of Applied Climate Science (ICACS), University of Southern Queensland, Springfield 4300, Australia;2. Department of Electrical and Electronics Engineering, Siirt University, 56100 Siirt, Turkey;1. State Key Laboratory of Solidification Processing, Northwestern Polytechnical University, Xi''an 710072, China;2. School of Physics and Electronic Engineering, Linyi University, Linyi 276005, China;3. Institute for Materials Research, Tohoku University, 2-1-1 Katahira, Sendai, Miyagi, 980-8577, Japan;1. Centre for Epidemiology and Public Health, Health Service and Population Research Department, Institute of Psychiatry, Psychology & Neuroscience, King''s College, London, UK;2. Research Institute for Primary Care and Health Sciences, Keele University, Staffordshire, UK;3. Institute for Research and Development, Colombo, Sri Lanka;4. Faculty of Medical Science, Anglia Ruskin University, UK;5. Department of Psychiatry and Psychology, School for Mental Health and Neuroscience, Maastricht University, The Netherlands |
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| Abstract: | The UDP-glucuronosyltransferase activity towards 4-nitrophenol, 1-naphthol and phenolphthalein was measured from the hepatic microsomes of the reindeer (Rangifer tarandus tarandus) after summer, autumn and winter feeding periods. The microsomes were digested with trypsin or digitonin. The UDP-glucuronosyltransferase activity with 4-nitrophenol and 1-naphthol as aglycones was lower in reindeer on winter food than in ones on summer food after trypsin and digitonin digestion. The activity towards phenolphthalein was the same in each feeding period. The different seasonal feeding affects the structure of microsomal membranes and this is reflected as modifications of the UDP-glucuronosyltransferase towards different substrates. |
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