Bovine Cu/Zn-Superoxide Dismutase,Cu/Zn-SOD ELISA Kit

1. Results indicate that variants of the PRLH and SOD1 genes are associated with heat tolerance in Chinese cattle. PMID: 30079537
2. The three-dimensional structure of bSOD1 reveals the imidazole ring of His19 localized within 5A from the alpha-carbon of Gly31 providing a structural basis that copper ion, most likely coordinated by His19, catalyzes the specific cleavage reaction PMID: 26872685
3. SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability PMID: 25416864
4. antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase, which show the changes in their expression during improper placental release PMID: 23398331
5. Results sugget thet Copper/Zinc superoxide dismutase (SOD1) may play a role in controlling intraluteal prostaglandin F2alph and reactive oxygen species action during functional and structural luteolysis. PMID: 23101731
6. ALOX5AP, CPNE3, IL1R2, IL6, TLR2, TLR4, and THY1 were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows. PMID: 20072847
7. Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced by PGF during functional luteolysis. PMID: 20519832
8. At room temperature (25.0 degrees C) and higher, the addition of high concentrations of polymer is found to significantly enhance the affinity of SOD for catalase. PMID: 20682270
9. Capillary electrophoresis and mass spectrometry to study the different structures of bovine SOD-1. In both cases, an average molecular mass corresponding to the apo-monomer SOD-1 was calculated. PMID: 20411580
10. flexibility of the metal sites involved in present a single-crystal X-ray diffraction study of Cu,Zn superoxide dismutase in space group P212121 at 0.57 GPa. The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution. PMID: 20516618
11. expression profile in follicles: oocytes (SOD1 throughout ooplasm & nucleoplasm); cumulus cells (no SOD1 detected); granulosa cells (expressed SOD1); follicular fluid (small follicles show increased amounts of SOD1 in comparison with large follicles) PMID: 20197373
12. Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions. PMID: 14688234
13. Raman spectrum analysis strongly suggests that the His41-mediated hydrogen bond bridge of Cu-Zn superoxide dismutase plays a crucial role in keeping the protein structure suitable for highly efficient catalytic reactions. PMID: 15096035
14. HCO(3)(-)-derived oxidant does not alter significantly the Cu(II) active site geometry and histidine coordination to Cu(II) in SOD1 as does H(2)O(2) alone PMID: 15123612
15. copper- and carbonate radical anion-mediated oxidations have roles in hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation PMID: 15607903
16. SOD1 mutants gain fatty acid binding abilities based on their structural instability and form cytotoxic granular aggregates PMID: 15799963
17. The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing 10(-4) M EDTA. PMID: 16202231
18. Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). PMID: 17042490
19. communication between the two monomers of SOD1 such that the binding of one zinc ion per homodimer has a more profound effect on the homodimeric protein structure than the binding of subsequent metal ions PMID: 17381088
20. DNA accelerates the formation of SOD1 aggregates and is incorporated into SOD1 aggregates. SOD1 association with DNA, driven by electrostatic interactions, can restrict the orientation of SOD1 molecules and increase a SOD1 population along DNA strands. PMID: 17469801
21. The results suggest that under cellular conditions ( approximately 5 mM bicarbonate) zinc-deficient SOD1 peroxidation could play a pathogenic role in neurodegenerative diseases. PMID: 17729118
22. The expression of SOD1 and SOD2 through the course of the estrous cycle is reported. PMID: 18572235
23. diminished hepatic protein nitration in the SOD1-/- mice was not directly related to plasma nitrite and nitrate concentrations PMID: 18573333
24. DNAs tested are simultaneously condensed into a nanoparticle with a specific morphology during SOD1 aggregation, revealing that SOD1 aggregation and DNA condensation are two concurrent phenomena. PMID: 18690666
25. Peroxymonocarbonate (HOOCO(2)(-)) is a key intermediate in the SOD1 peroxidase cycle and identify this species as the precursor of carbonate radical anions. PMID: 19286663

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KEGG: bta:281495

STRING: 9913.ENSBTAP00000032384

UniGene: Bt.49637