Detail of "474-86-2"

Reference

Determination of conjugated estrogens in pharmaceuticals

Determination of conjugated estrogens in pharmaceuticals. Agbaba, Danica; Zivanov-Stakic, Dobrila; Kovacevic, Milenija (Inst. Pharm. Chem., Fac. Pharm., Belgrade, Yugoslavia). Arh. Farm., 33(4), 159-65 (Serbo-Croatian) 1983. CODEN: ARFMAC. ISSN: 0004-1963. DOCUMENT TYPE: Journal CA Section: 64 (Pharmaceutical Analysis) Estrone [53-16-7], equilin [474-86-2], equilenin [517-09-9], 17a-estradiol [57-91-0], 17b-estradiol [50-28-2], 17a-dihydroequilin [651-55-8] and 17a-dihydroequilenin [6639-99-2] were sepd. and identified by TLC on silica gel. The compds. were detd. in bulk, Premarin tablets and Premarin-coated tablets. 3-Acetylaminobenzaldehyde thiosemicarbazone, and estrone was detd. by Kobes's reaction.

Structure-activity relationships of sex steroid analogs determined in vitro in a thyroid hormone-responsive membrane calcium-ATPase model

Structure-activity relationships of sex steroid analogs determined in vitro in a thyroid hormone-responsive membrane calcium-ATPase model. Lawrence, William D.; Osawa, Yoshio M.; Davis, Paul J.; Blas, Susan D. 72-63-9 and 846-48-0 are also occured in this study. (Hematol. Endocrinol. Div., Veterans Adm. Med. Cent., Buffalo, NY 14215, USA). Endocrinology (Baltimore), 119(6), 2803-8 (English) 1986. CODEN: ENDOAO. ISSN: 0013-7227. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Physiol. concns. of L-T4 [51-48-9] stimulate Ca2+-ATPase [9000-83-3] activity in vitro in reticulocyte membranes from female rabbits and inhibit this enzyme in reticulocyte membranes from males. Preincubation of intact cells or ghosts with testosterone [58-22-0] (5 ′ 10-11M) converted female-source reticulocyte membranes to male-type responsiveness to thyroid hormone (inhibition of Ca2+-ATPase activity). Preincubation of reticulocyte membranes with 17b-estradiol [50-28-2] (5 ′ 10-11M) converted male-source membranes to female-type responsiveness (stimulation by L-T4 of membrane Ca2+-ATPase activity). Using this sex steroid-sensitive thyroid hormone-dependent membrane enzyme system, the structure-activity relationships of analogs of sex steroids and unrelated steroids were examd. 5b-Androstanes were active compared to testosterone in assays using female-source membranes, whereas 5a-androstanes were less active. Within the 5b-androstanes, activity was dependent on 31 hydroxl group at the C3- or C17-position. Nongonadal steroids tested were less active, establishing specificity of the sex steroid effect in assays using female-source membranes. Assayed in male-source membranes, estrone [53-16-7] and 3-hydroxy-1,3,5-(10)7-estratetraen-17-one (equilin) [474-86-2] were active compared for estrogen effect with 17b-estradiol, whereas estriol [50-27-1] was less active. The activities of hydrocortisone [50-23-7] and aldosterone [52-39-1] were 76% and 71%, resp., in this system. These structure-activity relationships are distinct from those described for gonadal steroid-cytoplasmic binding proteins or nuclear interactions, and represent a novel sex steroid-thyroid hormone effect on activity of a membrane enzyme. .