Pub. Date : 1997 Oct 15
PMID : 9359420
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Thiocyanate and chloride as competing substrates for myeloperoxidase. | thiocyanate | myeloperoxidase | Homo sapiens |
| 2 | The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. | thiocyanate | myeloperoxidase | Homo sapiens |
| 3 | Our aim was to establish whether myeloperoxidase oxidizes thiocyanate in the presence of chloride at physiological concentrations of these substrates. | thiocyanate | myeloperoxidase | Homo sapiens |
| 4 | The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. | thiocyanate | myeloperoxidase | Homo sapiens |
| 5 | The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. | thiocyanate | myeloperoxidase | Homo sapiens |
| 6 | In the presence of 100 mM chloride, myeloperoxidase catalysed the production of hypothiocyanite at concentrations of thiocyanate as low as 25 microM. | thiocyanate | myeloperoxidase | Homo sapiens |
| 7 | The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 microM thiocyanate was added, and was maximal with 1mM thiocyanate. | thiocyanate | myeloperoxidase | Homo sapiens |
| 8 | The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 microM thiocyanate was added, and was maximal with 1mM thiocyanate. | thiocyanate | myeloperoxidase | Homo sapiens |
| 9 | This indicates that at plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated. | thiocyanate | myeloperoxidase | Homo sapiens |
| 10 | We conclude that thiocyanate is a major physiological substrate of myeloperoxidase, regardless of where the enzyme acts. | thiocyanate | myeloperoxidase | Homo sapiens |