High impact information on EQUILENIN

• Cotransfection experiments using estrogen receptor (ERalpha and/or ERbeta) expression vectors have indicated that neither receptor can potentiate the Eqn-mediated induction of apoA-I promoter activity [1].
• Transient transfection studies with human apoA-I promoter constructs derived from pGL3-luciferase reporter plasmid were used to identify the cis-acting element involved in Eqn-mediated induction [1].
• The results demonstrated that the apoA-I electrophile/antioxidant response element (EpRE/ARE) might be responsible for the increase in apoA-I promoter activity by Eqn [1].
• The separation of selected oestrogens (oestrone, equilin, alpha-oestradiol, beta-oestradiol and d-equilenin) using capillary supercritical fluid chromatography (SFC) was studied [2].
• An acetate at position 3 of d-equilenin is rapidly hydrolysed by tissue esterase and the liberated d-equilenin couples with a diazonium salt to form a coloured precipitate [3].

Biological context of EQUILENIN

• Both E1 and E2 remained at low levels until Day 80, increased significantly (P less than 0-05) by Day 120 to reach peak levels at Day 210 or 240 and then declined until parturition [4].
• Moreover, the emission of equilenine is completely quenched by I-, in contrast with the napththyl-1-phenylamine and perylene probes, which clearly demonstrates the accessibility of the catalytic site to water molecules and ions [5].
• The comparison of the fluorescence polarization changes of perylene and equilenine (a competitive inhibitor of the isomerase) with the ionic concentration indicates that there is no direct relation between the bulk lipidic phase and the enzymatic binding site properties [5].

Associations of EQUILENIN with other chemical compounds

• Levels of oestrone, equilin and equilenin (E1), oestradiol (E2) LH, PMSG and prolactin were measured by radioimmunoassay in serum from pregnant mares [4].

References