...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Mitochondrial creatine kinase binding to phospholipids decreases fluidity of membranes and promotes new lipidinduced #beta# structures as monitored by red edge excitation shift,laurdan fluorescence ,and FTIR
【24h】

Mitochondrial creatine kinase binding to phospholipids decreases fluidity of membranes and promotes new lipidinduced #beta# structures as monitored by red edge excitation shift,laurdan fluorescence ,and FTIR

机译：对磷脂的线粒体肌酸激酶结合降低了膜的流动性，并促进了通过红色激发换档，Laurdan荧光和FTIR监测的新脂质诱导的#β结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Structural modifications induced by the binding of mitochondrial creatine kinase (mtCK) to saturated and unsaturated phospholipids were monitored by using Laurdan, a membrane probe sensitive to the polarity of the environment. The abrupt change characteristic of a phase transition of lipids alone was attenuated by addition of mtCK. Generalized polarization spectra indicated that mtCK surface binding changed the phospholipid liquid-crystalline state to a more rigid state. Infrared spectra of lipids further strengthened these results: upon mtCK binding, the phospholipid methylene chains had a more rigid conformation than that observed without mtCK at the same temperature. After mtCK binding to vesicles of perdeuterated dimyristoylphosphatidylcholine and nondeuterated dimyristoylphosphatidylglycerol, no lateral phase separation was observed, suggesting that both lipids were rigidified. Moreover, mtCK bound to liposomes exhibited an uncommon red edge excitation shift of 19 nm, while that of the soluble enzyme was only 6 nm. These results indicated that the environment of some mtCK tryptophan residues was motionally restricted. Strong stabilization of the enzyme structure against heat denaturation was observed upon lipid binding. In addition, lipids promoted a new reversible protein—protein or protein—lipid interaction, as evidenced by infrared data showing a slight modification of the #beta# sheet over iix helix ratio with formation of a new 1632-cm~(-1) #beta# sheet instead of the soluble protein 1636-cm~(-1) one. Such modifications, inducing a decrease in the fluidity of the mitochondrial membranes, may play a role in vesicle aggregation; they could be implicated in the appearance of contact sites between internal and external mitochondrial membranes.
机译：通过使用Laurdan监测由Laurdan进行线粒体肌酸激酶（MTCK）与饱和和不饱和磷脂的结合诱导的结构修饰，对环境极性敏感的膜探针。通过添加MTCK衰减单独脂质的相转变的突然变化特征。广义偏振光谱表明MTCK表面结合将磷脂液晶状态改变为更刚性的状态。脂质的红外光谱进一步加强了这些结果：在MTCK结合时，磷脂亚甲基链具有比在相同温度下没有MTCK的情况下观察到的刚性构象。在MTCK与丙二酰磷磷苷酰磷苷酰氨基葡萄球菌和Nondeuterated Divyristoylphosphat磷脂酰氨基的结合后，未观察到横向相分离，表明两种脂质都刚性化。此外，与脂质体结合的MTCK表现出19nm的罕见红边励磁偏移，而可溶性酶的罕见是6nm。这些结果表明，一些MTCK色氨酸残留物的环境被致动限制。在脂质结合时观察到酶结构抵抗热变性的强稳定性。此外，脂质促进了一种新的可逆蛋白质 - 蛋白质或蛋白质 - 脂质相互作用，如红外数据所证明的，显示在IIX螺旋比与形成新的1632-cm〜（-1）＃ β＃薄片代替可溶性蛋白质1636-cm〜（-1）一。这种修饰，诱导线粒体膜的流动性降低，可能在囊泡聚集中发挥作用;它们可以暗示在内部和外部线粒体膜之间的接触部位的外观。

著录项

  • 来源
    《Biochemistry》 |2001年第20期|共11页
  • 作者

    Thierry Granjon; Marie-Jeanne Vacheron; Christian Vial; Rene Buchet;

  • 作者单位

    Laboratorie de Biomembranes et Enzymes Associes and Laoratoire de Physico-Chimie Biologique UMR 5013 "Reconnaissance et Transduction moleculaires"Universite Claude Bernard Lyon 1 69622 Villeurbanne Cedex France;

    Laboratorie de Biomembranes et Enzymes Associes and Laoratoire de Physico-Chimie Biologique UMR 5013 "Reconnaissance et Transduction moleculaires"Universite Claude Bernard Lyon 1 69622 Villeurbanne Cedex France;

    Laboratorie de Biomembranes et Enzymes Associes and Laoratoire de Physico-Chimie Biologique UMR 5013 "Reconnaissance et Transduction moleculaires"Universite Claude Bernard Lyon 1 69622 Villeurbanne Cedex France;

    Laboratorie de Biomembranes et Enzymes Associes and Laoratoire de Physico-Chimie Biologique UMR 5013 "Reconnaissance et Transduction moleculaires"Universite Claude Bernard Lyon 1 69622 Villeurbanne Cedex France;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

相似文献

  • 外文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号