Uterine peroxidase as a marker for estrogen action.

Uterine peroxidase as a marker for estrogen action.
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子宫过氧化物酶作为雌激素作用的标志物。

DOI:
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发表时间:
1977
影响因子:
11.1
通讯作者:
E. Desombre
E. Desombre
中科院分区:
综合性期刊1区
文献类型:
--
作者:
C. Lyttle;E. Desombre

文献摘要

被引文献

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给未成熟大鼠单剂量雌二醇可引起子宫内出现大量过氧化物酶(供体:过氧化氢氧化还原酶,EC 1.11.1.7)酶活性。这种酶的诱导作用被放线菌素D和环己亚胺抑制,在雌二醇给药后4小时可以检测到,在20小时达到最高水平,随后下降。单次给药后20小时子宫过氧化物酶的数量随着雌二醇的剂量从0.1微克增加到100微克。雌酮和雌三醇对过氧化物酶的诱导也表现出剂量依赖性,对这些类固醇的定量过氧化物酶反应遵循它们的子宫向性能力。抗雌激素CI628本身具有低水平的酶诱导能力,对雌激素诱导有抑制作用。子宫酶与二价阳离子,特别是钙的增溶,导致过氧化物酶的产量大幅增加。这种提取方法提供了大约50,000分子量的酶,区别于通常用氯化钠提取得到的大聚集形式。
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 hr, and thereafter declines. The amount of uterine peroxidase seen at 20 hr after a single dose increases with dose from 0.1 to 100 microgram of estradiol. Estrone and estriol also show dose-dependent induction of peroxidase, and the quantitative peroxidase responses to these steroids follow their uterotropic capacities. The antiestrogen CI628, capable of low levels of enzyme induction by itself, can inhibit the induction due to estrogen. Solubilization of the uterine enzyme with divalent cations, especially calcium, results in a substantially increased yield of peroxidase. This extraction method provides an enzyme of about 50,000 molecular weight in distinction to the large aggregated form obtained by the usual extraction with sodium chloride.