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Erythrocytic uridine diphosphate galactose in galactosaemia [PDF]
SummaryAn earlier claim of a deficiency of uridine diphosphate galactose in erythrocytes of galactosaemia patients was not confirmed. Enzymic techniques similar to those of the earlier investigators were used to determine not only the concentration of uridine diphosphate galactose but also the ratio of this concentration to the sum of the uridine sugar
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Measurements of uridine diphosphate glucose and uridine diphosphate galactose — an appraisal
European Journal of Pediatrics, 1995The recent disproof of a major deficiency of uridine diphosphate galactose in galactosemia should not lead investigators to assume either that enzymatic methods are unreliable for uridine sugar assays or that a defect in galactosylation in galactosemia has been excluded.
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STRUCTURE AND FUNCTION OF URIDINE DIPHOSPHATE GLUCURONOSYLTRANSFERASES
Clinical and Experimental Pharmacology and Physiology, 1997SUMMARY1. The uridine diphosphate (UDP)‐glucuronosyltransferases (UGT) are a family of enzymes that catalyse the covalent addition of glucuronic acid to a wide range of lipophilic chemicals. They play a major role in the detoxification of many exogenous and endogenous compounds by generating products that are more polar and, thus, more readily excreted
Robyn Meech, Peter I. Mackenzie
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Deficit of uridine diphosphate galactose in galactosaemia
Journal of Inherited Metabolic Disease, 1989SummaryThe levels of uridine diphosphate galactose (UDPGal) and uridine diphosphate glucose (UDPGlc) have been determined in liver autopsy samples, erythrocytes and cultured skin fibroblasts from galactosaemic patients and compared to non‐galactosaemic controls.
Yan-Kang Xu+7 more
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Synthesis of uridine diphosphate [1-3H]glucose and uridine diphosphate [6-3H]glucose
Chemistry of Natural Compounds, 1987Information is given on the synthesis of tritium-labeled UDPG by the successive transformation of D-[1-3H]glucose or D-[6-3H]glucose by the action of the enzymes hexokinase (EC 2.7.1.1), phosphoglucomutase (EC 2.7.5.1), and UDPG-pyrophosphorylase (EC 2.7.7.9) under conditions ensuring the retention of the tritium label.
L. S. Gordeeva+3 more
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, 2016
Despite the unsurpassed selectivity that enzymes usually offer, biocatalytic transformations repeatedly fall short of the robustness and process efficiency demanded for production-scale chemical synthesis.
Alexander Gutmann, B. Nidetzky
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Despite the unsurpassed selectivity that enzymes usually offer, biocatalytic transformations repeatedly fall short of the robustness and process efficiency demanded for production-scale chemical synthesis.
Alexander Gutmann, B. Nidetzky
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1963
Publisher Summary This chapter describes the isolation of uridine diphosphate glucose, uridine diphosphate acetylglucosamine, and guanosine diphosphate mannose. The basic principle is that alcoholic extract from toluene-autolyzed yeast is fractionated on anion-exchange columns.
Enrico Cabib, Luis F. Leloir
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Publisher Summary This chapter describes the isolation of uridine diphosphate glucose, uridine diphosphate acetylglucosamine, and guanosine diphosphate mannose. The basic principle is that alcoholic extract from toluene-autolyzed yeast is fractionated on anion-exchange columns.
Enrico Cabib, Luis F. Leloir
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Enzyme Kinetics of Uridine Diphosphate Glucuronosyltransferases (UGTs)
2021Glucuronidation, catalyzed by uridine diphosphate glucuronosyltransferases (UGTs), is an important process for the metabolism and clearance of many lipophilic chemicals, including drugs, environmental chemicals, and endogenous compounds. Glucuronidation is a bisubstrate reaction that requires the aglycone and the cofactor, UDP-GlcUA.
Upendra A. Argikar+2 more
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Archives of Biochemistry and Biophysics, 1975
Abstract Rat liver microsomes showed very active uridine diphosphate-galactose pyrophosphatase activity leading to the hydrolysis of uridine diphosphate-galactose into galactose1-phosphate and finally into galactose. The activity was observed in presence of buffers with wide ranges of pH.
James W.M. Yung, Sailen Mookerjea
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Abstract Rat liver microsomes showed very active uridine diphosphate-galactose pyrophosphatase activity leading to the hydrolysis of uridine diphosphate-galactose into galactose1-phosphate and finally into galactose. The activity was observed in presence of buffers with wide ranges of pH.
James W.M. Yung, Sailen Mookerjea
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Uridine diphosphate glucose dehydrogenase of calf liver
Biochemical Pharmacology, 1971Abstract UDP-glucose dehydrogenase of calf liver dissociated in guanidine-HCl into six subunits. The number of reactive sulfhydrylgroups of native and guanidine-HCl-treated enzyme was found to be 20 ± 1 and 46 ± 1, respectively, per mole of native enzyme.
Donald W. Visser+2 more
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