URIDINE DIPHOSPHATE ACETYLGALACTOSAMINE IN LIVER
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چکیده
منابع مشابه
Preparation of uridine diphosphate-N-acetylgalactosamine from uridine diphosphate-N-acetylglucosamine by using microbial enzymes.
A method was developed for the large scale preparation of uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc) from uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) by means of microbial enzymes. With Bacillus subtilis cell-free extract as a source of UDP-GlcNAc 4-epimerase, about 35% of the UDP-GlcNAc added was converted to UDP-GalNAc. After the residual UDP-GlcNAc was degraded to uridin...
متن کاملEnzymatic Synthesis of Uridine Diphosphate Xylose and Uridine Diphosphate Arabinose.
It has been shown previously' that mung bean seedlings contain a mixture of sugar nucleotides consisting of UDPG,2 UDPGal, UDPXy, and UDPAr. In the present communication evidence is presented that these bean seedlings contain an enzymatic system capable of catalyzing the reversible formation of UDPXy and UDPAr from UTP and a-D-Xy-l-P. When a-D-Xy-l-P and UTP were incubated in the presence of an...
متن کاملUridine Diphosphate Glucose Dehydrogenase
J-Hydroxyuridine cliphosphate glucose was prepared enzymatically and 5,Bdihydrouridine diphosphate glucose was prepared by the catalytic reduction of UDP-glucose. The effectiveness of these cofactor analogues as substrates for UDP-glucose dehydrogenase was determined. The rate of oxidation of 5-hydroxyuridine diphosphate glucose was onesixth that of UDP-glucose at pH 8.7 and one-half that of UD...
متن کاملStudies on the purification of rat liver uridine diphosphate glucuronyltransferase.
1. A stable, more highly purified, preparation of UDP-glucuronyltransferase was obtained than previously reported. 2. Enzyme activity towards o-aminophenyl and p-nitrophenyl was increased 43- and 46-fold respectively. 3. The final preparation contains only three staining polypeptide bands visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 4. The only known major accompany...
متن کاملThe heterogeneity of uridine diphosphate glucuronyltransferase from rat liver.
1. The glucuronide conjugation of p-nitrophenol, phenolphthalein, o-aminophenol and 4-methylumbelliferone by rat liver microsomes has been studied. The detergent Triton X-100 activated UDP-glucuronyltransferase activity towards all these substrates, therefore the optimum activating concentration was added in all experiments. 2. Mg(2+) enhanced the conjugation of the substrates. 3. With phenolph...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1955
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)52296-7