Zobrazeno 1 - 10
of 47
pro vyhledávání: '"P H, JELLINCK"'
Publikováno v:
Canadian Journal of Biochemistry. 53:855-860
The effect of various phenols on the conversion of [4-14C]estradiol to water-soluble products by estrogen-induced uterine peroxidase (EC 1.11.1.7) has been investigated. Evidence was provided that those phenols which enhanced the oxidation of estradi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1677234b04fb2e3f7d9b82c9043e7960
https://doi.org/10.1139/o75-116
https://doi.org/10.1139/o75-116
Autor:
S Kimura, P H Jellinck
Publikováno v:
Biochemical Journal. 205:271-279
A peroxidase, purified from rat small intestine to apparent homogeneity as judged by polyacrylamide-gel electrophoresis, exhibited an absorbance ratio (A412/A280) of 0.783. Its Mr (44000 +/- 1000) and spectral properties were similar to those of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1235ccde3a67e3a83c983ef6e1bd5913
https://doi.org/10.1042/bj2050271
https://doi.org/10.1042/bj2050271
Autor:
J H Bowen, P H Jellinck
Publikováno v:
Biochemical Journal. 185:129-137
1. The trans-epoxide of diethylstilboestrol and its pinacolone were synthesized chemically and the pinacolone shown to be formed from the epoxide by a non-enzymic process. 2. [14C]Diethylstiboestrol epoxide was converted by rat liver microsomal fract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05e75f19f8363b78d5b65b1f834c5b2b
https://doi.org/10.1042/bj1850129
https://doi.org/10.1042/bj1850129
Autor:
C. R. Lyttle, P. H. Jellinck
Publikováno v:
Biochemical Journal. 160:237-241
The distribution of oestrogen-induced peroxidase in the resuspended 8000g pellet of rat uterine homogenates was examined by centrifugation in a sucrose density gradient. Within 10h of treatment with oestradiol, peroxidase activity was found in a regi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a4673bea9a7d988a5b4374f6f0fc5cc
https://doi.org/10.1042/bj1600237
https://doi.org/10.1042/bj1600237
Autor:
P H Jellinck, T McNabb
Publikováno v:
Biochemical Journal. 151:275-279
1. An enzyme that can be induced in rat uteri by oestrogens and that catalyses the oxidation of guaiacol and the metabolism and binding of [4-14C]oestradiol to protein in the presence of H2O2 was partially purified by (NH4)2SO4 fractionation and poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e06a302ec278943d225ed1a7fb867e42
https://doi.org/10.1042/bj1510275
https://doi.org/10.1042/bj1510275
Publikováno v:
Journal of Biological Chemistry. 261:7729-7732
Release of 3H2O from regiospecifically labeled estradiol was measured during 2-hydroxylation of this estrogen by rat liver microsomes. The amount of tritium remaining in the isolated catechol estrogen was also determined. Virtually all the tritium wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f00ec13f5a123dec24342c3864c9499c
https://doi.org/10.1016/s0021-9258(19)57461-0
https://doi.org/10.1016/s0021-9258(19)57461-0
Autor:
Janette Woo, P. H. Jellinck
Publikováno v:
Journal of Endocrinology. 39:99-104
SUMMARY Oestrone administered in the form of subcutaneous pellets produced marked changes in the metabolism of [14C]oestradiol by male rat liver microsomes. The high yield of both 2-hydroxyoestradiol and water-soluble metabolites was decreased to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28dbd17ca2921d974caf69578820457b
https://doi.org/10.1677/joe.0.0390099
https://doi.org/10.1677/joe.0.0390099
Autor:
B. J. Brown, P. H. Jellinck
Publikováno v:
Biochemical Journal. 124:91-97
1. Oestradiol hydroxylase activity, as measured by the formation of water-soluble products, was significantly higher in the smooth endoplasmic reticulum of rat liver than in the rough membrane. 2. The isolated membrane fractions retained their activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49a18b374a760c78b631653d02d26e75
https://doi.org/10.1042/bj1240091
https://doi.org/10.1042/bj1240091
Autor:
P. H. Jellinck, C. R. Lyttle
Publikováno v:
Biochemical Journal. 127:481-487
1. An enzyme that catalyses the metabolism and binding of [4-14C]oestradiol to protein and to other high-molecular-weight substances in the presence of H2O2 was shown to be absent from the uteri of immature rats and to be induced by physiological dos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66225669d3b108fe9a313365a3a505c7
https://doi.org/10.1042/bj1270481
https://doi.org/10.1042/bj1270481
Autor:
P. H. Jellinck, Catherine Lazier
Publikováno v:
Canadian Journal of Biochemistry. 43:281-290
Inhibition studies with compounds having structural features in common with the natural estrogens have shown that 2-hydroxyestrone and 2-hydroxyestradiol are potent inhibitors of the rat liver microsomal system, which converts estrone to water-solubl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0350e3dc85cecb5af05dd25c2e5ef8f1
https://doi.org/10.1139/o65-035
https://doi.org/10.1139/o65-035