Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.17.3.2 (xanthine oxidase)
 8,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neoxanthin, a major carotenoid pigment of spinach, is found in the Chloroplast membrane and has an unknown function in plants. Neoxanthin inhibited the production of superoxide anions in an artificial xanthine and xanthine oxidase system and depressed DNA synthesis in methylcholanthrene (MCA)-initiated C3H10T1/2 fibroblasts. in two-stage carcinogenesis experiments, neoxanthin at 0.2 micrograms/0.2 ml inhibited the formation of tumors that were induced sequentially by 7,12-dimethylbenz[a]anthracene (DMBA) and 12-O-tetradecanoylphorbol-13-acetate (TPA) in the buccal pouch of Syrian Golden hamsters. To assess the ongoing process of carcinogenesis, the activity of ornithine decarboxylase (ODC), required for cell proliferation, was analyzed. Neoxanthin inhibited the activity of ODC when animals were treated with neoxanthin one hour before the application of TPA in two-stage carcinogenesis. However, neoxanthin did not inhibit ODC activity when animals were treated with neoxanthin one hour before the application of DMBA in two-stage carcinogenesis, and there was no subsequent tumor formation. In a short-term anti-initiation experiment, neoxanthin inhibited the covalent binding of isotope-labeled DMBA to DNA by 53%. These results indicate that neoxanthin inhibits the initiation stage and the promotion stage in two-stage carcinogenesis. This suggests that neoxanthin may act as a potential chemopreventive agent.
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PMID:The inhibition of DMBA-induced carcinogenesis by neoxanthin in hamster buccal pouch. 861 51

The molybdenum cofactor (Moco) is essential for the activity of all molybdoenzymes except nitrogenase. The cDNA for the Moco carrier protein (MocoCP) of Chlamydomonas reinhardtii has been cloned by reverse transcription PCR approaches with primers designed from microsequenced peptides of this protein. The C. reinhardtii MocoCP has been expressed in Escherichia coli. The recombinant protein has been purified to electrophoretic homogeneity and is found assembled into a homotetramer when Moco is not present under native conditions. Recombinant MocoCP has the same biochemical characteristics as MocoCP from C. reinhardtii, as it bound Moco from milk xanthine oxidase with high affinity, prevented Moco inactivation by oxygen, and transferred Moco efficiently to aponitrate reductase from the Neurospora crassa nit1 mutant. The genomic DNA sequence corresponding to the Chlamydomonas MocoCP gene, CrMcp1, also was isolated. This gene contained three introns in the coding region. The deduced amino acid sequence of CrMcp1 did not show a significant identity to functionally known proteins in the GenBank data base, although a significant conservation was found with bacterial proteins of unknown function. The results suggest that proteins having a Moco binding function probably exist in other organisms.
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PMID:Mcp1 encodes the molybdenum cofactor carrier protein in Chlamydomonas reinhardtii and participates in protection, binding, and storage functions of the cofactor. 1251 77