Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Utpalendu S. Maitra"'
Publikováno v:
Endocrinology. 133:1817-1822
The corticosteroid-binding globulin (CBG) receptor of rat hepatic membranes was solubilized using 1.5% Triton X-100. An assay for its activity was developed that was dependent upon the fact that the [125I] CBG-receptor complex adsorbs to hydroxylapat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2d964904dad4e38ba293a4fe5c5d955
https://doi.org/10.1210/endo.133.4.8404624
https://doi.org/10.1210/endo.133.4.8404624
Publikováno v:
Endocrinology. 127:278-284
This investigation was undertaken to ascertain whether rat liver cells contained a receptor for corticosteroid-binding globulin (CBG) that could be differentiated clearly from the asialoglycoprotein receptor. To do this, [125I]CBG, [125I] asialo-CBG,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffd9f8c496fb9ae341a712f32aca9534
https://doi.org/10.1210/endo-127-1-278
https://doi.org/10.1210/endo-127-1-278
Publikováno v:
Journal of Biological Chemistry. 249:3075-3078
The rates of epimerization of UDP-[4-3H]glucose, UDP-[4-3H]galactose, and UDP-[4-3H]xylose with UDP-galactose 4-epimerase from Escherichia coli and that of UDP-[4-3H]glucuronate with UDP-galacturonate 4-epimerase from Anabaena flos-aquae were determi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b56f634885668af3880d272f5b7dfc5
https://doi.org/10.1016/s0021-9258(19)42639-2
https://doi.org/10.1016/s0021-9258(19)42639-2
Publikováno v:
Steroids. 53:597-605
Labeled 4,4-dimethyl-5 alpha -cholesta-8,24-dien-3 beta-ol (4,4-dimethylzymosterol) was prepared by incubating labeled mevalonate with rat liver extracts in the presence of arsenite and lanosterol.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3950d5680394765dc8179a2baeb144b2
https://doi.org/10.1016/0039-128x(89)90034-2
https://doi.org/10.1016/0039-128x(89)90034-2
Publikováno v:
Journal of Biological Chemistry. 249:2366-2372
Epimerization of UDP-glucuronate to UDP-galacturonate in the blue-green alga Anabaena flos-aquae is catalyzed by an enzyme distinct from UDP-galactose 4-epimerase. Partially purified UDP-galacturonate 4-epimerase from this organism has the following
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6dca1d3afcd9d1a86c988863fc51c541
https://doi.org/10.1016/s0021-9258(19)42739-7
https://doi.org/10.1016/s0021-9258(19)42739-7
Autor:
Helmut Ankel, Utpalendu S. Maitra
Publikováno v:
Biochemical and Biophysical Research Communications. 32:526-532
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::482444d9fce5acb00bf297e81f5f7631
https://doi.org/10.1016/0006-291x(68)90694-3
https://doi.org/10.1016/0006-291x(68)90694-3
Autor:
Helmut Ankel, Utpalendu S. Maitra
Publikováno v:
Proceedings of the National Academy of Sciences. 68:2660-2663
When UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli is incubated with UDP-galactose, then reduced with NaB 3 H 4 , label is found in UDP-glucose and UDP-galactose. Enzymatic and chemical degradation demonstrates that the label is bound
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ee44451d246782a88a6b67adcc4cf11
https://doi.org/10.1073/pnas.68.11.2660
https://doi.org/10.1073/pnas.68.11.2660
Autor:
Utpalendu S. Maitra, Helmut Ankel
Publikováno v:
Journal of Biological Chemistry. 248:1477-1479
Incubation of UDP-galactose with substrate amounts of UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli for different times between 2 and 120 min, followed by reduction with NaB3H4 invariably yields a mixture of labeled UDP-glucose and UDP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a8d87bdd99dbe9eadb56dba4b792d1f
https://doi.org/10.1016/s0021-9258(19)44324-x
https://doi.org/10.1016/s0021-9258(19)44324-x
Autor:
Yoshiaki Oyama, Teruhisa Noguchi, Masaji Ishiguro, Yuzo Yoshida, Takehiro Oshima, Ritsuko Hatanaka, David B. Sprinson, Yuri Aoyama, Seiichi Imajo, Nobuhiro Ishida, Hiroshi Nakazato, Utpalendu S. Maitra, Venkitachalam P. Mohan
Publikováno v:
Biochemical and biophysical research communications. 155(1)
Genes for lanosterol 14-demethylase, cytochrome P450(14DM), and a mutated inactive cytochrome P450SG1 were cloned from S. cerevisiae strains D587 and SG1, respectively. A single nucleotide change resulting in substitution of Asp for Gly-310 of cytoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f010890ad8b686756d47010d038ab439
https://pubmed.ncbi.nlm.nih.gov/3046615
https://pubmed.ncbi.nlm.nih.gov/3046615
Autor:
L. Ponticorvo, David B. Sprinson, V.P. Mohan, H. Kochi, M. Adlersberg, K.-P. Liu, V. Shankar, Utpalendu S. Maitra
Publikováno v:
Biochemical and biophysical research communications. 108(2)
Oxygenation of the α-methyl group at C-4 (C-30) of lanosterol in solubilized rat liver microsomes was studied by 3 H release from [C-30- 3 H]-4, 4′-dimethylzymosterol. This activity required oxygen, a cyanide sensitive non-heme iron protein which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50c30c695fcfe4dc4c4e0464cf212eee
https://pubmed.ncbi.nlm.nih.gov/6816234
https://pubmed.ncbi.nlm.nih.gov/6816234