Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.5.1 extracted from

  • Yu, C.A.; Yu, L.
    Isolation and properties of a mitochondrial protein that converts succinate dehydrogenase into succinate-ubiquinone oxidoreductase (1980), Biochemistry, 19, 3579-3585.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bos taurus
-
succinate dehydrogenase
-

Purification (Commentary)

Purification (Comment) Organism
isolation from the soluble cytochrome b-c1 complex of the mitochondrial protein, which converts soluble succinate dehydrogenase into succinate-ubiquinone oxidoreductase using two different methods, method 1: treatment with Triton X-100 in the presence of urea, column chromatography on calcium phosphate and ammonium sulfate fractionation, method 2: ammonium acetate fractionation in the presence of deoxycholate, ammonium sulfate fractionation in the presence of urea, and differential centrifugation Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Subunits

Subunits Comment Organism
tetramer heart, succinate dehydrogenase, SDS-PAGE Bos taurus