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线粒体膜结合精氨酸酶的钾离子依赖性释放似乎是精氨酸酶-II的一种新变体。

KCl-Dependent Release of Mitochondrial Membrane-Bound Arginase Appears to Be a Novel Variant of Arginase-II.

作者信息

Suman Mishra, Rajnikant Mishra

机构信息

Biochemistry and Molecular Biology Laboratory, Department of Zoology, Banaras Hindu University, Varanasi 221005, India.

出版信息

Scientifica (Cairo). 2016;2016:3675283. doi: 10.1155/2016/3675283. Epub 2016 May 16.

DOI:10.1155/2016/3675283
PMID:27293971
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4884806/
Abstract

Arginase regulates arginine metabolism, ornithine-urea cycle, and immunological surveillance. Arginase-I is predominant in cytosol, and arginase-II is localised in the mitochondria. A mitochondrial membrane-bound arginase has also been proposed to be adsorbed with outer membrane of mitochondria which gets released by 150 mM potassium chloride (KCl). It is presumed that inclusion of 150 mM KCl in the homogenization medium would not only facilitate release of arginase bound with outer membrane of mitochondria but also affect functional anatomy of mitochondria, mitochondrial enzymes, and proteins. Therefore, it has been intended to characterize KCl-dependent release of mitochondrial membrane-bound arginase from liver of mice. Results provide advancement in the area of arginase biology and suggest that fraction of mitochondrial membrane-bound arginase contains mitochondrial arginase-II and a variant of arginase-II.

摘要

精氨酸酶调节精氨酸代谢、鸟氨酸-尿素循环和免疫监视。精氨酸酶-I主要存在于细胞质中,而精氨酸酶-II定位于线粒体。也有人提出一种线粒体膜结合精氨酸酶与线粒体外膜吸附,可被150 mM氯化钾(KCl)释放。据推测,在匀浆介质中加入150 mM KCl不仅会促进与线粒体外膜结合的精氨酸酶的释放,还会影响线粒体的功能结构、线粒体酶和蛋白质。因此,旨在表征小鼠肝脏中线粒体膜结合精氨酸酶的氯化钾依赖性释放。结果为精氨酸酶生物学领域提供了进展,并表明线粒体膜结合精氨酸酶部分含有线粒体精氨酸酶-II和精氨酸酶-II的一种变体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/83c1b502b414/SCIENTIFICA2016-3675283.008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/67ed5df53f67/SCIENTIFICA2016-3675283.001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/6c6a67c8f4dc/SCIENTIFICA2016-3675283.002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/a510da55283c/SCIENTIFICA2016-3675283.003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/2666ef61faeb/SCIENTIFICA2016-3675283.004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/8cef9ff0bbaf/SCIENTIFICA2016-3675283.005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/f40dec5a698b/SCIENTIFICA2016-3675283.006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/30fd7d8e9432/SCIENTIFICA2016-3675283.007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/83c1b502b414/SCIENTIFICA2016-3675283.008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/67ed5df53f67/SCIENTIFICA2016-3675283.001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/6c6a67c8f4dc/SCIENTIFICA2016-3675283.002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/a510da55283c/SCIENTIFICA2016-3675283.003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/2666ef61faeb/SCIENTIFICA2016-3675283.004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/8cef9ff0bbaf/SCIENTIFICA2016-3675283.005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/f40dec5a698b/SCIENTIFICA2016-3675283.006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/30fd7d8e9432/SCIENTIFICA2016-3675283.007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f84/4884806/83c1b502b414/SCIENTIFICA2016-3675283.008.jpg

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