oxalates and 4-cresol
oxalates has been researched along with 4-cresol* in 2 studies
Other Studies
2 other study(ies) available for oxalates and 4-cresol
| Article | Year |
|---|---|
In vitro methylation of arsenite by rabbit liver cytosol: effect of metal ions, metal chelating agents, methyltransferase inhibitors and uremic toxins.
The methylation of carrier-free 74As-arsenite by liver cytosol of Flemish Giant rabbits is highly susceptible to additions of trace elements. In vitro supplementation of essential trace elements like zinc (Zn2+), vanadium (V5+), iron (Fe2+), copper (Cu2+) and selenate was shown to increase the methylation efficiency. Trivalent metal ions (e.g. Al3+, Cr3+ and Fe3+), Hg2+, Tl+ and SeO3(2-) had a deleterious effect. The inhibitory effect of EDTA, oxime and many divalent cations (Ca2+, Mg2+, Sr2+, ...) suggest a co-factor role for a specific divalent metal ion, possibly Zn2+. Chelating agents used in clinical treatment of acute and chronic inorganic arsenic poisoning lower the methylation capacity of cytosol by rendering the trivalent arsenic unavailable for the methyltransferase enzymes. S-adenosylhomocysteine and periodate-oxidized adenosine, inhibitors of s-adenosylmethionine dependent methylation pathways, inhibit the methylation of arsenite. Pyrogallol, a catechol-O-methyltransferase inhibitor, blocks the action of arsenite- and monomethylarsonic methyltransferase enzymes, suggesting a close structural relationship between the active sites of the different enzymes. Some uraemic toxins, namely oxalate, p-cresol, hypoxanthine, homocysteine and myo-inositol, inhibit arsenic methylation. Topics: Animals; Arsenites; Cresols; Cytosol; Edetic Acid; Enzyme Inhibitors; Homocysteine; Hypoxanthine; In Vitro Techniques; Inositol; Liver; Male; Metals, Heavy; Methylation; Oxalates; Pyrogallol; Rabbits; Radioisotopes; S-Adenosylhomocysteine; Substrate Specificity; Uremia | 1999 |
Binding of horseradish, lignin, and manganese peroxidases to their respective substrates.
The present study utilizes 1H NMR spectroscopy to characterize the binding of substrate to heme active site of three different peroxidases, horseradish peroxidase, lignin peroxidase, and manganese peroxidase. Information has been obtained on the site of p-cresol binding to the active-site cavity of the cyanide derivative of horseradish peroxidase. This information was obtained by relaxation enhancements of the substrate protons and connectivities between the latter and heme 8-CH3 and a Phe residue. Manganese(II) is shown to bind to ferri-manganese peroxidase and its cyanide derivative in a specific site with a high-affinity constant (10(4) M-1). Manganese(II) binding exhibits a slow exchange rate with respect to the difference in T2(-)1 of the affected signals in the manganese(II)-containing and manganese(II)-free species. Manganese(II) affects the line width of certain heme methyl resonances and of certain one-proton intensity signals in manganese peroxidase and its cyanide derivative. The behavior of MnP toward manganese(II) is compared to that of the closely related peroxidase, lignin peroxidase (LiP), with its native substrate veratryl alcohol. LiP does not have a specific binding site for manganese(II). Topics: Benzyl Alcohols; Binding Sites; Calcium; Cresols; Cyanides; Horseradish Peroxidase; Kinetics; Magnetic Resonance Spectroscopy; Manganese; Oxalates; Oxalic Acid; Peroxidases; Protein Binding | 1993 |