Changes and Their Control Mechanisms of Mitochondrial Electron-Transport Components During Ascaris Life Cycle

蛔虫生命周期线粒体电子传递成分的变化及其控制机制

基本信息

批准号：
01570223
负责人：
TAKAMIYA Shinzaburo
金额：
$ 1.34万
依托单位：
Juntendo University School of Medicine
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1989
资助国家：
日本
起止时间：
1989 至 1990
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-01570223/
关键词：
Ascaris Mitochondria Respiratory chain Complex II Life cycle Cytochrome Larva Quinone ミトクロム

项目摘要

1. The primary structure of the flavin-bound tryptic peptide from the Fp subunit of Ascaris adult complex II was determined and found to be highly similar to those of the corresponding flavin-binding regions of bovine heart and bacterial Fp subunits.The Ascaris Fp subunit was shown to contain two regions exhibiting striking sequence similarity to the segments interacting with the AMP moiety of FAD in bacterial Fp subunits.2. To elucidate mechanisms of aerobic-anaerobic respiratory transition during development of Ascaris nematode, the larval respiratory chain and its complex II (succinate-ubiquinone oxidoreductase) have been characterized in the isolated mitochondria by spectrophotometry, immunoblotting using anti adlt complex II antibodies and determination of quinones.The results obtained showed that L_2 larvae were the most aerobic among stages studied and the larval complex II was different from the adults counterpart. Furthermore, evidence showing biosynthetic conversion of quinones during development was obtained.3. Oxidation-reduction midpoint potentials (Ems) were determined at pH 7.0 for cytochromes in the anaerobic respiratory chain of Ascaris mitochondria by redox titration techniques.Cytochrome b_<558>, which is associated with complex II that functions as fumarate reductase in the terminal step of the respiratory chain, was shown to have an Em of -34 mV in the isolated complex II and -54 mV in mitochondria. These values are much higher than the value reported for mammalian cytochrome b_<560> of complex II, showing a unique feature of Ascaris cytochrome b_<558>.

1。确定了从阿斯卡里斯成人成年复合物II的FP亚基中的黄素结合胰蛋白酶肽的主要结构，并发现与牛心脏的相应黄素结合区域高度相似亚基2。为了阐明在ass骨线虫发展过程中有氧运动型呼吸过渡的机制，幼虫呼吸链及其复合物II及其复合物II（琥珀酸 - 偶联氧化酶）在分离的线粒体中通过光谱测定法表征了分离的线粒体，通过光谱测定法，使用抗adlt a抗毒性和确定为II II抗体，并确定QUININE in II II _2在研究的阶段和幼体综合体II中，最有氧运动与成年人不同。此外，获得了发育过程中喹酮生物合成转化的证据。3。通过氧化还原滴定技术在pH 7.0的pH 7.0确定氧化中的中点电位（EMS）的氧化呼吸道链，通过氧化还原滴定技术（Cytotrome b_ <558>）与fumarate Repeffert ini Indepried Indepried Insipratient Is the Em she EM相关的Cytotrome b_ <558>，该复合物与II II函数相关联，该复合物与fumarate Repeffert sembs in em相关。线粒体中-54 mV。这些值远高于复合物II的哺乳动物细胞色素B_ <560>报告的值，显示了Ascaris细胞色素B_ <558>的独特特征。