Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sulfite oxidase (EC 1.8.3.1), purified from chicken liver, is comprised of two identical subunits of 55 kDa, each of which contains a molybdenum and heme prosthetic group. The functional size of sulfite oxidase was determined by radiation inactivation analysis using both full, sulfite:cytochrome c reductase, and partial, sulfite:ferricyanide reductase, catalytic activities. Inactivation of full enzyme activity indicated a target size of 42 kDa while the partial activity indicated a target size of 25 kDa. These results confirm the earlier findings of two equivalent subunits and suggest the presence of a functional domain within the subunit structure that contains the molybdenum center and exhibits a smaller molecular mass than that of the enzyme subunit.
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PMID:Radiation inactivation of hepatic sulfite oxidase. 330 May 54

1. The sulfite oxidases from various vertebrates, including rat, rabbit, chicken, frog, and eel, were partially purified and their physiochemical, kinetic, and immunochemical properties compared. The physicochemical and kinetic properties of these five enzymes were similar. 2. Antibody against the molybdenum-containing peptide prepared from purified rat liver sulfite oxidase was raised in rabbits. In Ouchterlony double diffusion and quantitative immunoprecipitation tests, the antibody could form precipitates with the enzymes from rats and rabbits, but no reaction was observed with enzymes from other sources. 3. The sulfite-cytochrome c reductase activity of the enzymes from these five animals were inhibited by the antibody, though the enzymes from chicken, frog, and eel were less sensitive to the antibody than those from rat and rabbit. 4. The inhibition of binding between 3H-labeled rat sulfite oxidase and its antibody by unlabeled enzymes from other animals demonstrated that 10 to 20% of the antibody could cross-react with these enzymes.
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PMID:Comparative immunochemical studies of sulfite oxidases of vertebrate livers. 716 Dec 65