Tissue-specific differences between heart and liver cytochrome c oxidase.
Tissue-specific differences between heart and liver cytochrome c oxidase.
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心脏和肝脏细胞色素 C 氧化酶之间的组织特异性差异。
DOI：
10.1021/bi00413a048
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
Capaldi,RA
中科院分区：
文献类型：
--
作者：
Yanamura,W;Zhang,YZ;Takamiya,S;Capaldi,RA
韦恩Yanamura，Yu-Zhong Zhang，Shinzaburo Takamiya和Roderick A. Capaldi* 分子生物学研究所，俄勒冈州大学，尤金，俄勒冈州97403接收于1988年1月8日;修订的Mandarin pt接收于1988年2月19日摘要：牛肝细胞色素c氧化酶已被分离，并将该制剂的亚基结构与牛心脏酶的亚基结构进行了比较。在10个核编码亚基中，3个在2种组织形式中不同，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中具有不同的迁移，对针对心脏亚基的抗体具有不同的抗原性，以及不同的N-末端氨基酸序列。心脏阿萨亚基起始于肝脏SSG的N-末端序列，在前33个残基中有17个不同，包括在该亚基的肝脏同种型中缺失2个残基。肝脏的亚基CVii与其心脏对应物在前37个残基中的6个不同，而来自肝脏的亚基CIX与心脏同种型在前25个残基中的15个不同。在其余核编码亚基的部分测序中未观察到组织类型之间的差异。最近，已通过克隆和测序该多肽的cDNA获得了大鼠肝脏CIX亚基序列的主要部分[Suske，G.，Mengel，T.，Cordingley，M.，& Kadenbach，B.（1987）Eur. 168，233-237]。CIX的大鼠和牛肝脏形式的序列同源性大于牛心脏和肝脏同种型之间的同源性。C-细胞色素c氧化酶，呼吸链的末端部分，催化分子氧还原为水，与质子穿过线粒体内膜的易位偶联[回顾于Capaldi et al.（1983）和Wikstrom et al.（1984）]。这样产生的质子梯度用于驱动离子运输或用于ATP合成。细胞色素c氧化酶是由3个细胞编码的多肽和10个核编码的亚基组成的完整膜复合物[回顾于Capaldi et al.（1987）和Kadenbach et al.（1987）]。最近的证据表明，三个氨基酸编码的亚基是酶的催化核心，含有辅基并参与质子泵送功能（Ludwig & Schatz，1980; Raitio等人，1987;霍尔姆等人，1987年）。核编码和胞质合成亚基的作用现在才开始被详细研究。现有证据表明，这些亚基中的一些参与催化活性的调节[综述见Kadenbach（1986）和Ka-denbach et al.（1987）]。
Wayne Yanamura, Yu-Zhong Zhang, Shinzaburo Takamiya, and Roderick A. Capaldi* Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403 Received January 8, 1988; Revised Manuscript Received February 19, 1988 abstract: Bovine liver cytochrome c oxidase has been isolated and the subunit structure of this preparation compared with that of the bovine heart enzyme. Of the 10 nuclear-coded subunits, 3 were different in the 2 tissue forms, having different migrations in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, different antigenicities to antibodies made against the heart subunits, and different N-terminal amino acid sequences. Subunit ASA of heart begins with the N-terminal sequence of SSG inliver and is different in17 of the first 33 residues including a deletion of 2 residues in the liver isoform of this subunit. Subunit CVii of liver differs from its heart counterpart in 6 of the first 37 residues while subunit CIX from liver differs from the heart isoform in 15 of the first 25 residues. No differences between tissue types were observed in partial sequencing of the remaining nuclear-coded subunits. Recently, the major portion of the sequence of subunit CIX from rat liver has been obtained by cloning and sequencing of the cDNA for this polypeptide [Suske, G., Mengel, T., Cordingley, M., & Kadenbach, B.(1987) Eur. J. Biochem. 168, 233-237]. There is a greater sequence homology of the rat and bovine liver forms of CIX than there is betweenthe bovine heart and liver isoforms.C-ytochrome c oxidase, the terminal part of the respiratory chain, catalyzes a reduction of molecular oxygento water, coupled to the translocation of protons across the mitochondrial inner membrane [reviewed in Capaldi et al.(1983) and Wikstrom et al.(1984)]. The proton gradient so generated is usedto drive ion transport or is used for ATP synthesis. Cytochrome c oxidase is an integral membrane complex composed of 3 mitochondrially coded polypeptides and 10 nuclear-coded subunits [reviewed in Capaldi et al.(1987) and Kadenbach et al.(1987)]. Recentevidence suggests that the three mitochondrially coded subunits are the catalytic core of the enzyme, containing the prosthetic groups and involved in the proton pumping function (Ludwig & Schatz, 1980; Raitio et al., 1987; Holm et al., 1987). The role of the nuclear-coded and cytoplasmically synthesized subunits is just now beginning to be explored in any detail. The available evidence suggests that some of these subunits are involved in regulation of catalytic activity [reviewed in Kadenbach (1986) and Ka-denbach et al.(1987)].
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影响因子：
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作者：
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作者：
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影响因子：
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作者：
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DOI：
--
发表时间：
1986
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Wright,RM;Dircks,LK;Poyton,RO
通讯作者：
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