The effect of unsaturated fatty acids on the rate of synthesis of rat liver glucose-6-phosphate dehydrogenase
Autor: | Marianne Frolich, Darold Holten, Engin M. Gozukara |
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Rok vydání: | 1972 |
Předmět: |
Male
Time Factors media_common.quotation_subject Biophysics Appetite Dehydrogenase Glucosephosphate Dehydrogenase Biology Biochemistry Antigen-Antibody Reactions chemistry.chemical_compound Animals Glucose-6-phosphate dehydrogenase adipocyte protein 2 Molecular Biology media_common chemistry.chemical_classification Immune Sera Body Weight Fatty acid Fasting Diet Rats Kinetics Glucose Enzyme Liver chemistry Fatty Acids Unsaturated biology.protein Rabbits Branched-chain alpha-keto acid dehydrogenase complex Polyunsaturated fatty acid |
Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 286:155-163 |
ISSN: | 0304-4165 |
DOI: | 10.1016/0304-4165(72)90101-8 |
Popis: | 1. 1. Rat liver glucose-6-phosphate dehydrogenase has been used to test the hypotheses that unsaturated fatty acids inhibit this enzyme in vivo or act as co-pressors regulating the synthesis of lipogenic enzymes. When rats are switched from a non-fat diet to one containing 15% fatty acid there is an 8-fold decrease in the level of glucose-6-phosphate dehydrogenase. Quantitative precipitation of the enzyme with an antiserum against glucose-6-phosphate dehydrogenase established that this 8-fold decrease was due to a decrease in the amount of enzyme protein rather than an inhibition of preexisting enzyme. 2. 2. A kinetic method was used to determine the rate of glucose-6-phosphate dehydrogenase synthesis and degradation in the presence of dietary fatty acids. It is concluded that dietary fatty acids decrease the rate of synthesis of glucose-6-phosphate dehydrogenase. Alterations in the levels of glucose and fatty acid in the diet lead to the conclusion that fatty acids act indirectly by decreasing the appetite. These results do not support the hypothesis that polyunsaturated fatty acids act as co-repressors to regulate the synthesis of lipogenic enzymes. |
Databáze: | OpenAIRE |
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