Methaemoglobin Content and NADH-methaemoglobin Reductase Activity of Three Human Erythrocyte Genotypes

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methaemoglobin content and nadh-methaemoglobin reductase activity of three human erythrocyte genotypes

background: to study methaemoglobin content and nadh-methaemoglobin reductase activity of three human erythrocyte genotypes (hbaa, hbas and hbss).materials and methods: studies to ascertain methaemoglobin concentration and level of nadh-methaemoglobin reductase activity of three human erythrocyte genotypes (hbaa, hbas and hbss) were carried out in forty-three (43) healthy male participants of c...

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Methaemoglobin as an Indicator of PMOR Activity

MetHb is often defined as oxidised Hb; that is the haem iron is oxidised from the ferrous (Fe) state to the ferric (Fe) state. In addition, in metHb the sixth coordination site of the haem iron is liganded to a water molecule; this shifts the absorbance maxima from that of Hb causing metHb to be chocolate brown in colour (acid form). At pH ~8 the water molecule is replaced by a bound hydroxyl g...

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Mechanism of methaemoglobin reduction by human erythrocytes.

The time course of methaemoglobin reduction in human erythrocytes treated with nitrite was studied at pH 7.4, 37 degrees C, in the presence or absence of Methylene Blue, and the changes in methaemoglobin, intermediate haemoglobins and oxyhaemoglobin during the reaction were analysed by isoelectric-focusing on Ampholine/polyacrylamide-gel plates. In both cases, with or without the dye, the inter...

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The interaction of inositol hexaphosphate with methaemoglobin.

1. Inositol hexaphosphate causes the shape of the oxidation-reduction equilibrium curve to become hyberbolic at acid pH values. 2. Inositol hexaphosphate also causes a decrease in the alkaline oxidation Bohr effect at these same pH values. 3. These results support the idea that inositol hexaphosphate causes methaemoglobin to take up the deoxyhaemoglobin quaternary structure at pH6.5.

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ژورنال

عنوان ژورنال: Asian Journal of Biochemistry

سال: 2010

ISSN: 1815-9923

DOI: 10.3923/ajb.2011.98.103