Purification and immunochemical characterization of a low-pI form of UDP glucuronosyltransferase from mouse liver
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Cited by (45)
Hetero-oligomer formation of mouse UDP-glucuronosyltransferase (UGT) 2b1 and 1a1 results in the gain of glucuronidation activity towards morphine, an activity which is absent in homo-oligomers of either UGT
2020, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The blots were incubated in 2% skim milk in 20 mM Tris-buffered saline (pH 7.5) containing 0.1% Tween 20 (TBS-T) for 30 min, and further incubated overnight with primary antibodies diluted 2,000-fold in 5% skim milk TBS-T at 4 °C. The primary antibodies used are rabbit anti-UGT2B7, mouse anti-α-tubulin (Proteintech, Rosemont, IL), goat anti-mouse low pI Ugt [19], rabbit anti-rat UGT1A [20], and rabbit anti-UGT2B21 as prepared above. The blots were extensively washed with TBS-T, and also incubated with horse radish peroxidase (HRP)-conjugated secondary antibodies; HRP-donkey anti-rabbit IgG and HRP-sheep anti-mouse IgG (GE Healthcare, Little Chalfont, UK), and HRP-rabbit anti-goat IgG (Biomedicals, Santa Ana, CA).
Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification
2011, Journal of Biological ChemistryCitation Excerpt :COS-1 and mouse SYF fibroblast cells were grown in DMEM with 4 and 10% fetal bovine serum, respectively. Antibodies against 2B7 were as follows: anti-UGT-1168 (25) detected protein backbone, and anti-Tyr(P)-438–2B7, generated by Syn-Pep (Dublin, CA), detected only Tyr(P)-438–2B7. Anti-Fgr was from Cell Signaling Technology.
Src supports UDP-glucuronosyltransferase-2B7 detoxification of catechol estrogens associated with breast cancer
2009, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Phosphorylated Y438 peptide [CKRVINDPSY(P03)KENV] derived from 2B7 was used to generate rabbit antibody (SynPeP), which was preabsorbed against nonphosphorylated peptide and then positively purified over phosphorylated peptide-containing resin. Anti-UGT-1168 was generated against highly purified Ugt2b5 [24]; it was again examined for specificity (P.S. Mitra/N.K. Basu, K. Chakraborty, and I.S. Owens, Manuscript ready for submission). Again, it showed no signal in nontransfected COS-1 cells (see Fig. 2C).
Fatty acyl-CoA as an endogenous activator of UDP-glucuronosyltransferases
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The digestion was performed for 30 min at 20 °C and then 50 μg trypsin inhibitor in 5 μl Buffer A was added to the incubation mixture to terminate digestion. Then, the samples were subjected to Western blotting [18,19] with a non-selective anti-UGT antibody [20] or anti-UGT2B1 antibody [21]. Immunochemical staining was performed with alkaline phosphatase-labeled secondary antibody according to the method of Blake et al. [22].
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Present address: Laboratory of Vision Research, National Eye Institute, National Institutes of Health, Bethesda, Md. 20205.