• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

人类子宫肌层的收缩蛋白。

The contractile proteins of the human myometrium.

作者信息

Cavaille F

出版信息

Acta Physiol Hung. 1985;65(4):453-60.

PMID:4013777
Abstract

The contractile proteins of the human myometrium were quantified and characterized in order to investigate their possible modifications during pregnancy. The myosin concentration was found to be 1 to 5 mg/g of tissue, while actin concentration ranged from 16 to 60 mg/g, leading to an actin/myosin ratio higher (Mean = 14) than in other smooth muscles. Purified myosin submitted to two-dimensional gel electrophoresis exhibited two isoelectric forms for the 17 KD Light Chain, the more acidic being predominant in the pregnant organ, the more basic in the non gravid one. The mobility of myosin of form filaments was studied using electron microscopy. Only the myosin purified from gravid uteri in its phosphorylated form did aggregate in long bipolar filaments. Actin was characterized in crude muscle extracts using two-dimensional gel electrophoresis. It appeared in three forms differing by their isoelectric points. The more basic form (gamma) predominates in the pregnant organ, as soon as 17 weeks of pregnancy, while in the non-pregnant uterus it is the intermediate (beta) form which is predominant.

摘要

为了研究人类子宫肌层收缩蛋白在孕期可能发生的变化,对其进行了定量和特性分析。结果发现,肌球蛋白浓度为每克组织1至5毫克,而肌动蛋白浓度在每克16至60毫克之间,导致肌动蛋白与肌球蛋白的比例(平均值为14)高于其他平滑肌。经二维凝胶电泳分析,纯化后的肌球蛋白在17KD轻链上呈现出两种等电形式,酸性较强的形式在妊娠子宫中占主导,碱性较强的形式在未孕子宫中占主导。利用电子显微镜研究了丝状形式的肌球蛋白的迁移率。只有从妊娠子宫中纯化出的磷酸化形式的肌球蛋白会聚集成长的双极丝。利用二维凝胶电泳对粗制肌肉提取物中的肌动蛋白进行了特性分析。它呈现出三种等电点不同的形式。碱性较强的形式(γ)在妊娠17周后即在妊娠子宫中占主导,而在未孕子宫中占主导的是中间形式(β)。

相似文献

1
The contractile proteins of the human myometrium.人类子宫肌层的收缩蛋白。
Acta Physiol Hung. 1985;65(4):453-60.
2
Isoforms of myosin and actin in human, monkey and rat myometrium. Comparison of pregnant and non-pregnant uterus proteins.人、猴和大鼠子宫肌层中肌球蛋白和肌动蛋白的亚型。妊娠子宫与非妊娠子宫蛋白质的比较。
Eur J Biochem. 1986 Nov 3;160(3):507-13. doi: 10.1111/j.1432-1033.1986.tb10068.x.
3
Maturation of ovine uterine smooth muscle during development and the effects of parity.
J Soc Gynecol Investig. 2000 Sep-Oct;7(5):284-90.
4
Myosin heavy chain isoform expression in human myometrium: presence of an embryonic nonmuscle isoform in leiomyomas and in cultured cells.
Cell Motil Cytoskeleton. 1995;30(3):183-93. doi: 10.1002/cm.970300303.
5
Human skeletal muscle myosin light chains analyzed by immobilized pH gradients during ontogenesis: identification of new phosphorylatable isoforms of light chain 2.在个体发育过程中通过固定化pH梯度分析的人骨骼肌肌球蛋白轻链:轻链2新的可磷酸化异构体的鉴定
Electrophoresis. 1990 Apr;11(4):325-32. doi: 10.1002/elps.1150110411.
6
Characterization and comparison of the contractile proteins from human gravid and non-gravid myometrium.人妊娠和非妊娠子宫肌层收缩蛋白的特性与比较
Gynecol Obstet Invest. 1983;16(6):341-53. doi: 10.1159/000299293.
7
Muscle protein analysis by two-dimensional gel electrophoresis.通过二维凝胶电泳进行肌肉蛋白质分析。
Crit Rev Clin Lab Sci. 1982;18(1):79-109. doi: 10.3109/10408368209082590.
8
Up-regulation of myometrial RHO effector proteins (PKN1 and DIAPH1) and CPI-17 (PPP1R14A) phosphorylation in human pregnancy is associated with increased GTP-RHOA in spontaneous preterm labor.人妊娠期间子宫肌层RHO效应蛋白(PKN1和DIAPH1)的上调以及CPI-17(PPP1R14A)磷酸化与自发性早产中GTP-RHOA增加有关。
Biol Reprod. 2007 Jun;76(6):971-82. doi: 10.1095/biolreprod.106.058982. Epub 2007 Feb 14.
9
Preparation and P content of non-pregnant and pregnant human uterine myosin.非妊娠和妊娠人类子宫肌球蛋白的制备及磷含量
Acta Physiol Hung. 1986;68(2):147-57.
10
Differences in contractile protein content and isoforms in phasic and tonic smooth muscles.相平滑肌和紧张性平滑肌中收缩蛋白含量及亚型的差异。
Am J Physiol. 1998 Sep;275(3):C684-92. doi: 10.1152/ajpcell.1998.275.3.C684.