Metabolism of Pyrogallol to Purpurogallin by Human Erythrocytic Hemoglobin
نویسندگان
چکیده
منابع مشابه
Metabolism of pyrogallol to purpurogallin by human erythrocytic hemoglobin.
The aim of this study was to investigate the oxido-reductive reactions of human hemoglobin with pyrogallol and the metabolism of pyrogallol by the protein, which contains a protoporphyrin IX like cytochrome P-450. Pyrogallol, having three hydroxy groups at the adjacent positions in the benzene ring, oxidized human oxyhemoglobin to methemoglobin and reduced human methemoglobin to oxyhemoglobin. ...
متن کاملOxidation of pyrogallol to purpurogallin by crystallin catalase.
It has been recently reported that catalytic quantities of crystalline catalase, in the presence of hydrogen peroxide, can rapidly oxidize a variety of molecules larger than hydrogen peroxide and aliphatic alcohols (1). The qualitative experiments have shown that oc-naphthol and p-phenylenediamine are condensed by oxidative coupling to indophenol purple; p-aminobenzoic acid, sulfathiazole, adre...
متن کاملAntimelanogenic Effect of Purpurogallin in Murine Melanoma Cells
Melanin is one of the most important factors affecting skin color. Melanogenesis is the bioprocess of melanin production by melanocytes in the skin and hair follicles and is mediated by several enzymes, such as tyrosinase, tyrosinase related protein (TRP)-1, and TRP-2. Convenient enzymatic transformation of the simple phenol pyrogallol with polyphenol oxidase originating from pear to an oxidati...
متن کاملBinding of human hemoglobin by Haemophilus influenzae.
Binding of biotinylated human hemoglobin to Haemophilus influenzae was detected when organisms were grown in heme-deplete, but not heme-replete, conditions. Hemoglobin binding was completely inhibited by a 100-fold excess of unlabelled human hemoglobin or human hemoglobin complexed with human haptoglobin. Binding was only partially inhibited by rat hemoglobin, bovine hemoglobin, human globin, a...
متن کاملMetabolism of nomifensine to a dihydroisoquinolinium ion metabolite by human myeloperoxidase, hemoglobin, monoamine oxidase A, and cytochrome P450 enzymes.
Nomifensine is an antidepressant agent that was removed from use because of a high incidence of hemolytic anemia. It contains an N-methyl-8-aminotetrahydroisoquinoline ring which has the potential to be oxidized to quaternary dihydroisoquinolinium and isoquinolinium ions, albeit such a transformation had not been previously observed. In this report, we demonstrate the conversion of nomifensine ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Tohoku Journal of Experimental Medicine
سال: 2004
ISSN: 0040-8727,1349-3329
DOI: 10.1620/tjem.203.319