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前列腺素F2α与富含5-核苷酸酶、Ca2+-ATP酶和Mg2+-(Na++K+)ATP酶的膜组分的选择性结合。

Selective binding of prostaglandin F2 alpha to membrane fractions enriched in 5-nucleotidase, Ca2+-ATPase, and Mg2+-(Na+ + K+)ATPase.

作者信息

Tóth M, Asbóth G, Hertelendy F

出版信息

Endocrinology. 1981 Jul;109(1):106-12. doi: 10.1210/endo-109-1-106.

DOI:10.1210/endo-109-1-106
PMID:6113129
Abstract

Homogenates of uterine smooth muscle of laying hens were fractionated by differential centrifugation. Three of the five fractions thus obtained were further separated on sucrose gradient into four subfractions. By employing various enzyme markers, such as 5'-nucleotidase, Mg2+-(Na+ + K+)-ATPase, alkaline phosphatase, Ca2+-ATPase, cytochrome oxidase, acid phosphatase, and N-beta-acetyl glucosaminidase, the major subcellular fractions have been tentatively identified. Using gel filtration to separate bound and free prostaglandin F2 alpha (PGF2 alpha) we found that the specific uptake of PGF2 alpha was highest in the subfractions which also exhibited the highest enrichment in enzymes viewed generally as markers for cell membrane. The results suggest that PGF2 alpha-induced contractile activity in this tissue is initiated by the specific interaction of this agonist with discreet receptors in the sarcolemma, rather than by binding of PGF2 alpha to intracellular organelles or to a cytosolic receptor.

摘要

对产蛋母鸡子宫平滑肌匀浆进行差速离心分级分离。将由此获得的五个级分中的三个在蔗糖梯度上进一步分离成四个亚级分。通过使用各种酶标记物,如5'-核苷酸酶、Mg2+-(Na+ + K+)-ATP酶、碱性磷酸酶、Ca2+-ATP酶、细胞色素氧化酶、酸性磷酸酶和N-β-乙酰氨基葡萄糖苷酶,初步鉴定了主要的亚细胞级分。利用凝胶过滤分离结合型和游离型前列腺素F2α(PGF2α),我们发现PGF2α的特异性摄取在那些通常被视为细胞膜标记物的酶中富集程度也最高的亚级分中最高。结果表明,PGF2α在该组织中诱导的收缩活性是由该激动剂与肌膜中离散受体的特异性相互作用引发的,而不是由PGF2α与细胞内细胞器或胞质受体的结合引发的。

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Selective binding of prostaglandin F2 alpha to membrane fractions enriched in 5-nucleotidase, Ca2+-ATPase, and Mg2+-(Na+ + K+)ATPase.前列腺素F2α与富含5-核苷酸酶、Ca2+-ATP酶和Mg2+-(Na++K+)ATP酶的膜组分的选择性结合。
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引用本文的文献

1
Copurification of prostaglandin F2 alpha receptors with rat uterine plasma membranes.前列腺素F2α受体与大鼠子宫质膜的共纯化
Experientia. 1983 Oct 15;39(10):1102-3. doi: 10.1007/BF01943130.