1. Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart
- Author
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Fei Sun, Jianxing Xu, Yujia Zhai, Dan Su, Xia Huo, Xuemei Li, Mark Bartlam, Aojin Wang, and Zihe Rao
- Subjects
chemistry.chemical_classification ,Cellular respiration ,Protein subunit ,Peptide ,Cell Biology ,Biology ,Biochemistry ,Molecular biology ,Citric acid cycle ,chemistry.chemical_compound ,chemistry ,Oxidoreductase ,Molecular Biology ,Integral membrane protein ,Ethylene glycol ,Ammonium sulfate precipitation - Abstract
The mitochondrial respiratory complex II, or succinate:ubiquinone oxidoreductase, is an integral membrane protein complex in both the tricarboxylic acid cycle (Krebs cycle) and aerobic respiration. The gene sequences of each complex II subunit were measured by RT-PCR. N-terminal sequencing work was performed to identify the mitochondrial targeting signal peptide of each subunit. Complex II was extracted from porcine heart and purified by the ammonium sulfate precipitation method. The sample was solubilized by 0.5% (w/v) sugar detergent n-decyl-β-d-maltoside, stabilized by 200 mm sucrose, and crystallized with 5% (w/v) poly(ethylene glycol) 4000. Important factors for the extraction, purification and crystallization of mitochondrial respiratory complex II are discussed.
- Published
- 2007
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