| Autor: |
Waugh, William H. |
| Předmět: |
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| Zdroj: |
Journal of Applied Research; Spring2004, Vol. 4 Issue 2, p208-214, 7p, 1 Chart |
| Abstrakt: |
Nephelometric assays of human Cohn plasma protein fraction IV-1 (rich in glycoproteins and lipids) were performed at protein concentrations of 40 mg/dL of saline solutions after incubations with 40 µmol/L concentrations of H2O2. Induced turbidities were related to complete turbidities or insolubilities caused by 1.5 g/dL sulfosalicylic acid. Turbidity was induced when H2 O2 was incubated with 100 µmol/L ferrous ion levels. Mean protein insolubilities of 7.28 ± 0.33% (n=12) (P<0.001) were induced when the ferrous sulfate reacted with 40 µmol/L H2O2. H2O2 alone at 40 µmol/L did not induce turbidities. Of 6 amino acids tested at acidity close to that in active endosomes and lysosomes, only arginine and lysine, by binding to iron inhibited markedly protein insolubilities, induced by micromolar Fenton-type oxidative reactions. Histidine inhibited lessly. The inhibition was mediated by oxidation-reduction chelation of bivalent iron by dibasic amino acid. The findings give credence to the hypothesis that Fenton-type oxidative reactions in the choroid vasculature and retinal pigment epithelium may be important early in the pathogenesis of age-related macular degeneration. Macronutritional trial with arginine or its precursor, citrulline, may be warranted in this disease. [ABSTRACT FROM AUTHOR] |
| Databáze: |
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