منابع مشابه
Uterine peroxidase as a marker for estrogen action.
Administration of a single dose of estradiol to immature rats gives rise to the appearance of substantial amounts of peroxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) enzyme activity in the uterus. This enzyme induction, which is inhibited by administration of actinomycin D and cycloheximide, can be detected at 4 hr after administration of estradiol, reaches a maximum level by 20...
متن کاملsynthesis and characterization of some macrocyclic schiff bases
ماکروسیکلهای شیف باز از اهمیت زیادی در شیمی آلی و دارویی برخوردار می باشند. این ماکروسیکلها با دارابودن گروه های مناسب در مکانهای مناسب می توانند فلزاتی مثل مس، نیکل و ... را در حفره های خود به دام انداخته، کمپلکسهای پایدار تولید نمایند. در این پایان نامه ابتدا یک دی آلدئید آروماتیک از گلیسیرین تهیه می شود و در مرحله بعدی واکنش با دی آمینهای آروماتیک و یا آلیفاتیک در رقتهای بسیار زیاد منجر به ت...
15 صفحه اولZinc Oxide- Peroxidase Biosensor: Fabrication and Characterization
Zinc oxide nanocomposite was prepared by sol gel method. Synthesized nanoparticle was characterized by X-ray diffraction and FT-IR spectroscopy. According to XRD analysis the crystallite size was found to be 30nm (approx) for ZnO. The formation of ZnO is confirmed by FT-IR. ZnO is used for the preparation of HRP/ ZnO/PVA/Au electrode. ZnO nanocomposite is mixed with PVA Solution and a thin laye...
متن کاملCharacterization of porcine uterine estrogen sulfotransferase.
A quantitative trait locus (QTL) for uterine capacity is located on chromosome 8. Comparison of porcine and human genetic maps suggested that the estrogen sulfotransferase (STE) gene may be located near this region. The objectives of this study were to clone the full coding region for STE, compare endometrial STE gene expression between Meishan and White composite pigs during early pregnancy, a...
متن کاملPURIFICATION AND SOME PARTIAL CHARACTERIZATION OF PEROXIDASE ISOENZYME FROM BRASSICA OLERACEA CAPITATA L.
Acetone fractionated peroxidase from crude extract of Brassica oleracea leaves (Cabbage) was purified in three steps on chromatographic columns, using Sp-Sepharose, DEAE-Sepharose and Con A-Sepharose. The specific activity of purified main isoenzyme (BOC-POD) is 1887 u/mg protein with RZ: 3.1, which is 172 times more than the RZ of crude extract with 4.3% recovery. The molecular weight of BOC-P...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1958
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68056-7