Disease relevance of SDHC

• The QPs1 subunit of bovine heart mitochondrial succinate-ubiquinone reductase was overexpressed in Escherichia coli DH5 alpha cells as a glutathione S-transferase fusion protein (GST-QPs1) using the expression vector, pGEX/QPs1 [1].

High impact information on SDHC

• The partial amino-terminal sequence of this peptide is GLTISQL-, indicating that this tryptic peptide comprises amino acid residues 113-140 of the revised amino acid sequence of QPs1 [2].
• Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase [2].
• The [3H]azido-Q-labeled QPs1 was purified from labeled reductase by a procedure involving ammonium sulfate fractionation, dialysis, organic solvent extraction, lyophilization, preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and cold acetone precipitation [2].
• The structure of QPs1 was studied by immunochemistry and molecular cloning and sequencing [3].
• Assignment of the subunit C of succinate dehydrogenase complex (SDHC) gene to bovine chromosome 2 with somatic and radiation hybrid panel mapping [4].

Biological context of SDHC

• The molecular weight of QPs1, calculated from the deduced amino acid sequence, is 14,320 [3].
• Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase. Immunochemistry, cloning, and nucleotide sequencing [3].

Associations of SDHC with chemical compounds

• When isolated recombinant QPs1 is dispersed in 0.01% dodecyl maltoside, it is in a highly aggregated form with an apparent molecular mass of over 1 million [1].
• However, partial N-terminal amino acid sequence analysis of recombinant QPs1 shows two extra amino acid residues, glycine and serine, at the N-terminus of mature QPs1, resulting from the recombinant manipulation [1].

Analytical, diagnostic and therapeutic context of SDHC

• Antibodies against QPs1 were raised in rabbits, purified, and characterized by enzyme-linked immunosorbent assay and Western blotting [3].

References