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Molecular cloning of a chiral-specific 3 alpha-hydroxysteroid sulfotransferase

Publikováno v: The Journal of biological chemistry. 269(22)

A novel stereoselective hydroxysteroid sulfotransferase (HST) that acts on neutral steroids having the 3-hydroxyl group in the alpha orientation but not on steroids where the 3-hydroxyl group is oriented in the beta position has been cloned and expre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5133f4a229884180a184a0560c70e7b3
https://pubmed.ncbi.nlm.nih.gov/8195238

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Isolation of two distinct 3-hydroxysteroid sulfotransferases from the guinea pig adrenal. Evidence for 3 alpha-hydroxy versus 3 beta-hydroxy stereospecificity

Autor: W J, Driscoll, B M, Martin, H C, Chen, C A, Strott

Publikováno v: The Journal of biological chemistry. 268(31)

Two physically distinct hydroxysteroid sulfotransferases (HSTs) that demonstrate substrate specificity with respect to the orientation of the ring A 3-hydroxyl group have been isolated from the guinea pig adrenal gland. Nondenaturing liquid-phase iso

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a541cf674873c62dc79a8c6e4a838eba
https://pubmed.ncbi.nlm.nih.gov/8226877

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Purification and identification of the heat-stable factor required for pregnenolone-binding protein activity. Evidence that the factor is adenosine 3',5'-diphosphate

Autor: Y C, Lee, T, Oeda, W J, Driscoll, H M, Fales, C A, Strott

Publikováno v: The Journal of biological chemistry. 267(16)

This paper presents data identifying adenosine 3',5'-diphosphate (3',5'-ADP) as the small heat-stable factor essential for the active steroid binding complex of the adrenocortical pregnenolone-binding protein (PBP). Factor activity obtained from the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c2880d6acb3c112cec255ceef554c976
https://pubmed.ncbi.nlm.nih.gov/1597440

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Regulation of adrenocortical pregnenolone-binding protein activity by phosphorylation/dephosphorylation. Phosphatase-mediated inactivation is reversed by cytosolic kinase

Autor: W J, Driscoll, Y C, Lee, C A, Strott

Publikováno v: The Journal of biological chemistry. 265(21)

The pregnenolone-binding protein (PBP) in guinea pig adrenocortical cytosol is inactivated (converted to a nonsteroid-binding form) by incubation with calf intestinal alkaline phosphatase at pH 9. Previously bound pregnenolone does not prevent this i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c061ddffa3839f6d0fcb3f1772ccab1a
https://pubmed.ncbi.nlm.nih.gov/2165058

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Charge isoforms of the adrenocortical pregnenolone-binding protein: influence of phosphorylation on isoformation and binding activity

Autor: W J Driscoll, C A Strott, Y C Lee

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 87(5)

Isoelectric focusing of the Mr 34,000 pregnenolone-binding protein (PBP) isolated from the guinea pig adrenal cortex has revealed multiple charge isoforms. Alkaline phosphatase treatment resulted in the disappearance of the pI 5.4 isoform associated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34ab72981246112e986315595e1cd197
https://pubmed.ncbi.nlm.nih.gov/2308958

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A Specific Progesterone Receptor in the Hamster Uterus: Physiologic Properties and Regulation During the Estrous Cycle1

Autor: B. W. O′Malley, Wendell W. Leavitt, D. O. Toft, C. A. Strott

Publikováno v: Endocrinology. 94:1041-1053

Our previous studies indicated the presence of an estrogen-dependent, progesteronebinding system in the hamster uterus. A progesterone- binding component has now been characterized in the uterine cytosol fraction by density gradient centrifugation (6

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::71e85f08191dfea9008b66fb9935ece2
https://doi.org/10.1210/endo-94-4-1041

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A pregnenolone-binding protein in soluble fraction of guinea pig adrenal cortex

Autor: C A Strott

Publikováno v: Journal of Biological Chemistry. 252:464-470

A pregnenolone-binding component has been detected in the soluble fraction of the guinea pig adrenal cortex. Enzymatic degradation studies revealed that the binding component was a protein. The binding was destroyed at 60 degrees but was not inhibite

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2548d20feaf10e546fb0d0189c8da50a
https://doi.org/10.1016/s0021-9258(17)32739-4

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