The Experts below are selected from a list of 156 Experts worldwide ranked by ideXlab platform
Neil Kaplowitz - One of the best experts on this subject based on the ideXlab platform.
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identification purification and immunochemical characterization of a tocopherol binding protein in rat liver Cytosol
Journal of Lipid Research, 1992Co-Authors: H. Yoshida, M Yusin, John Kuhlenkamp, Andrew Stolz, T. Hirano, Neil KaplowitzAbstract:Tocopherol binding activity accompanying a rat liver Cytosolic protein with molecular weight of 30-36 kDa has been demonstrated previously, although the isolation of the protein has not been reported. We now report the purification of an a-tocopherol-binding protein (TBP) from rat liver Cytosol utilizing three chromatographic procedures: gel filtration, Affi-Gel Blue affinity chromatography, and chromatofocusing. Three peaks of specific a-tocopherol- binding activity were resolved on Mi-Gel Blue, referred to as AFB-lA, lB, and 2. A 32-kDa homogeneous form was ob- tained after chromatofocusing of AFB-1B. M-(~H) toco- pherol was displaced from homogeneous TBP in the presence of 500-fold excess of nonlabeled a-tocopherol, in- dicating the specificity of the binding. Anti-TBP rabbit an- tisera identified only one protein in rat hepatic Cytosol on Western blotting. TBP immunoreactivity was found in the Cytosol of rat liver and the lysate of fractionated hepatocytes, but not in the Cytosol of other organs (including the heart, spleen, testes, and lung) nor in the lysate of fractioned Ito cells, endothelial cells, or Kupffer cells isolated from rat liver. Semiquantitative ELISA demonstrated that rat liver Cytosol contained approximately 2 mg TBP/g of Cytosol pro- tein. This immunoreactivity was associated with only the 30- 36 kDa gel filtration fractions of rat liver Cytosol and with both AFBlA and -lB but not with AFB2.-Yoshida, H., M. Yusin, I. Ren, J. Kuhlenkamp, T. Hirano, A. Stolz, and N. Kaplowitz. Identification, purification, and immunochemical characterization of a tocopherol-binding protein in rat liver Cytosol. J. Lipid Res. 1992. 33: 343-350.
H. Yoshida - One of the best experts on this subject based on the ideXlab platform.
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identification purification and immunochemical characterization of a tocopherol binding protein in rat liver Cytosol
Journal of Lipid Research, 1992Co-Authors: H. Yoshida, M Yusin, John Kuhlenkamp, Andrew Stolz, T. Hirano, Neil KaplowitzAbstract:Tocopherol binding activity accompanying a rat liver Cytosolic protein with molecular weight of 30-36 kDa has been demonstrated previously, although the isolation of the protein has not been reported. We now report the purification of an a-tocopherol-binding protein (TBP) from rat liver Cytosol utilizing three chromatographic procedures: gel filtration, Affi-Gel Blue affinity chromatography, and chromatofocusing. Three peaks of specific a-tocopherol- binding activity were resolved on Mi-Gel Blue, referred to as AFB-lA, lB, and 2. A 32-kDa homogeneous form was ob- tained after chromatofocusing of AFB-1B. M-(~H) toco- pherol was displaced from homogeneous TBP in the presence of 500-fold excess of nonlabeled a-tocopherol, in- dicating the specificity of the binding. Anti-TBP rabbit an- tisera identified only one protein in rat hepatic Cytosol on Western blotting. TBP immunoreactivity was found in the Cytosol of rat liver and the lysate of fractionated hepatocytes, but not in the Cytosol of other organs (including the heart, spleen, testes, and lung) nor in the lysate of fractioned Ito cells, endothelial cells, or Kupffer cells isolated from rat liver. Semiquantitative ELISA demonstrated that rat liver Cytosol contained approximately 2 mg TBP/g of Cytosol pro- tein. This immunoreactivity was associated with only the 30- 36 kDa gel filtration fractions of rat liver Cytosol and with both AFBlA and -lB but not with AFB2.-Yoshida, H., M. Yusin, I. Ren, J. Kuhlenkamp, T. Hirano, A. Stolz, and N. Kaplowitz. Identification, purification, and immunochemical characterization of a tocopherol-binding protein in rat liver Cytosol. J. Lipid Res. 1992. 33: 343-350.
J S Lilleyman - One of the best experts on this subject based on the ideXlab platform.
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in vitro metabolism of 6 mercaptopurine by human liver Cytosol
Xenobiotica, 1999Co-Authors: K Rowland, L Lennard, J S LilleymanAbstract:1. The aim of this study was to investigate 6-mercaptopurine (6MP) metabolism by human liver Cytosol in vitro. 2. Cytosol was prepared from seven human livers (A-G). A single Cytosol (C) was used to optimize incubation conditions. 3. Cytosols A-G were incubated with 6MP at 2, 10 and 500 muM for two fixed times (5 and 48 h). Parent drug, thiopurine and thionucleotide metabolites were quantitated by high performance liquid chromatography at all time points. 4. At 5 and 48 h the 2 muM and 10 muM 6MP incubations contained both 6MP and its initial nucleotide metabolite, thioinosine 5'-monophosphate (TIMP). In addition, the 10 muM 6MP 48 h incubates contained small amounts of 6-thioguanine (6TG, median 0.12 muM). At 500 muM 6MP all seven liver incubates produced a range of metabolites. At 48 h these included thiouric acid, 8-hydroxy-6-mercaptopurine and 6-methylmercaptopurine (median 31, 19.5 and 8.8 muM respectively), with TIMP, 6TG, thioxanthine and thioxanthine nucleotide at median concentrations of 61, 0.79...
John Kuhlenkamp - One of the best experts on this subject based on the ideXlab platform.
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identification purification and immunochemical characterization of a tocopherol binding protein in rat liver Cytosol
Journal of Lipid Research, 1992Co-Authors: H. Yoshida, M Yusin, John Kuhlenkamp, Andrew Stolz, T. Hirano, Neil KaplowitzAbstract:Tocopherol binding activity accompanying a rat liver Cytosolic protein with molecular weight of 30-36 kDa has been demonstrated previously, although the isolation of the protein has not been reported. We now report the purification of an a-tocopherol-binding protein (TBP) from rat liver Cytosol utilizing three chromatographic procedures: gel filtration, Affi-Gel Blue affinity chromatography, and chromatofocusing. Three peaks of specific a-tocopherol- binding activity were resolved on Mi-Gel Blue, referred to as AFB-lA, lB, and 2. A 32-kDa homogeneous form was ob- tained after chromatofocusing of AFB-1B. M-(~H) toco- pherol was displaced from homogeneous TBP in the presence of 500-fold excess of nonlabeled a-tocopherol, in- dicating the specificity of the binding. Anti-TBP rabbit an- tisera identified only one protein in rat hepatic Cytosol on Western blotting. TBP immunoreactivity was found in the Cytosol of rat liver and the lysate of fractionated hepatocytes, but not in the Cytosol of other organs (including the heart, spleen, testes, and lung) nor in the lysate of fractioned Ito cells, endothelial cells, or Kupffer cells isolated from rat liver. Semiquantitative ELISA demonstrated that rat liver Cytosol contained approximately 2 mg TBP/g of Cytosol pro- tein. This immunoreactivity was associated with only the 30- 36 kDa gel filtration fractions of rat liver Cytosol and with both AFBlA and -lB but not with AFB2.-Yoshida, H., M. Yusin, I. Ren, J. Kuhlenkamp, T. Hirano, A. Stolz, and N. Kaplowitz. Identification, purification, and immunochemical characterization of a tocopherol-binding protein in rat liver Cytosol. J. Lipid Res. 1992. 33: 343-350.
M Yusin - One of the best experts on this subject based on the ideXlab platform.
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identification purification and immunochemical characterization of a tocopherol binding protein in rat liver Cytosol
Journal of Lipid Research, 1992Co-Authors: H. Yoshida, M Yusin, John Kuhlenkamp, Andrew Stolz, T. Hirano, Neil KaplowitzAbstract:Tocopherol binding activity accompanying a rat liver Cytosolic protein with molecular weight of 30-36 kDa has been demonstrated previously, although the isolation of the protein has not been reported. We now report the purification of an a-tocopherol-binding protein (TBP) from rat liver Cytosol utilizing three chromatographic procedures: gel filtration, Affi-Gel Blue affinity chromatography, and chromatofocusing. Three peaks of specific a-tocopherol- binding activity were resolved on Mi-Gel Blue, referred to as AFB-lA, lB, and 2. A 32-kDa homogeneous form was ob- tained after chromatofocusing of AFB-1B. M-(~H) toco- pherol was displaced from homogeneous TBP in the presence of 500-fold excess of nonlabeled a-tocopherol, in- dicating the specificity of the binding. Anti-TBP rabbit an- tisera identified only one protein in rat hepatic Cytosol on Western blotting. TBP immunoreactivity was found in the Cytosol of rat liver and the lysate of fractionated hepatocytes, but not in the Cytosol of other organs (including the heart, spleen, testes, and lung) nor in the lysate of fractioned Ito cells, endothelial cells, or Kupffer cells isolated from rat liver. Semiquantitative ELISA demonstrated that rat liver Cytosol contained approximately 2 mg TBP/g of Cytosol pro- tein. This immunoreactivity was associated with only the 30- 36 kDa gel filtration fractions of rat liver Cytosol and with both AFBlA and -lB but not with AFB2.-Yoshida, H., M. Yusin, I. Ren, J. Kuhlenkamp, T. Hirano, A. Stolz, and N. Kaplowitz. Identification, purification, and immunochemical characterization of a tocopherol-binding protein in rat liver Cytosol. J. Lipid Res. 1992. 33: 343-350.
