Results 161 to 170 of about 509,948 (192)
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Urinary steroid excretion in 17α-hydroxylase deficiency

Journal of Steroid Biochemistry, 1978
Abstract Urinary steroids from a patient with 17α-hydroxylase deficiency syndrome have been identified. The steroids were obtained by enzymatic hydrolysis of urine, Amberlite XAD-2 extraction and Sephadex LH-20 column chromatography. Following preparation of volatile derivatives, the steroids were separated and estimated by gas chromatography on open-
J. Tourniaire   +3 more
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Hydroxylation of steroids with 11α-hydroxylase of Rhizopus nigricans

Journal of Steroid Biochemistry, 1987
Three groups of 3-keto-4-ene steroids with different side chains were used as substrates for the induced 11 alpha-hydroxylase of Rhizopus nigricans. The highest total bioconversion as well as the highest yield of 11 alpha-hydroxylated product is found using progesterone as substrate.
Zakelj-Mavric M, Belic I
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The steroid 16α-hydroxylase system in mammalian liver

Steroids, 1966
Abstract The 16α-hydroxylation of testosterone and androst-4-ene-3, 17-dione (2) and of estradiol-17β (3) takes place in the presence of a microsomal fraction of rat liver. The rate of 16α-hydroxylation of 3β-hydroxyandrost-5-en-17-one (DHA) by liver slices is significantly higher for male than for female adult rats (4).
Antonio Colás   +2 more
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STEROID HYDROXYLASES IN LIVER MICROSOMES AND MITOCHONDRIA

1980
Publisher Summary This chapter provides an overview of steroid hydroxylases in liver microsomes and mitochondria. Several hydroxylases are involved in the conversion of cholesterol into cholic acid. One is cholesterol 7α–monooxygenase, which hydroxylates cholesterol at C7.
Yohko Atsuta   +3 more
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Molecular biology of steroid hydroxylase deficiency

Adolescent and Pediatric Gynecology, 1988
Abstract Recent advances in the molecular and cell biology of the steroid hydroxylase genes have begun to provide an explanation for the molecular basis of the steroid hydroxylase deficiencies. 21-Hydroxylase deficiency is one of the most frequent genetic diseases.
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Disorders of the Aldosterone Synthase and Steroid 11β-Hydroxylase Deficiencies

Hormone Research in Paediatrics, 1999
The most potent corticosteroids are 11β-hydroxylated compounds. In humans, two cytochrome P450 isoenzymes with 11β-hydroxylase activity, catalysing the biosynthesis of cortisol and aldosterone, are present in the adrenal cortex. CYP11B1, the gene encoding 11β-hydroxylase (P450c11), is expressed on high levels in the zona fasciculata and is regulated by
Peter, M   +2 more
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Steroid 16α‐Hydroxylase from Human Fetal Liver; Inhibition by Steroids

Acta Obstetricia et Gynecologica Scandinavica, 1980
The 16α‐hydroxylase system in fetal liver which used dehydroepiandrosterone (DHA) or pregnenolone as substrate, was apparently inhibited by various endogenous and synthetic steroids: DHA, pregnenolone, their sulfates, androstenediol, androstenetriol, estrone, estradiol‐17β, ethynylestradiol and chlormadinone‐acetate.
Yumiko Sano   +5 more
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Steroid 21 Hydroxylase Deficiency Congenital Adrenal Hyperplasia

Endocrinology and Metabolism Clinics of North America, 2009
Steroid 21 hydroxylase deficiency is the most common form of congenital adrenal hyperplasia (CAH). The severity of this disorder depends on the extent of impaired enzymatic activity, which is caused by various mutations of the 21 hydroxylase gene. This article reviews adrenal steroidogenesis and the pathophysiology of 21 hydroxylase deficiency.
Maria I. New   +2 more
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Heterogeneity of the Bovine Adrenal Steroid 21-Hydroxylase

Endocrine Research, 1989
The results presented indicate that purified cytochrome P-45021 which migrated upon SDS gel electrophoresis essentially as a single band, is further separable into different species by ion-exchange chromatography. The P-450 eluted from the CM-Sephadex column at different points along the buffer concentration gradient, exhibited significant differences ...
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Intracellular distribution and properties of steroid 11β-hydroxylase and steroid 18-hydroxylase in rat adrenal

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
Yutaka Nakamura, Bun-Ichi Tamaoki
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