Methaemoglobin Content and NADH-Methaemoglobin Reductase Activity of Three Human Erythrocyte Genotypes
نویسندگان: ثبت نشده
چکیده مقاله:
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 confirmed erythrocyte genotypes: HbAA (N=15), HbAS (N=15) and HbSS (N=13). Spectrophotometric method was used for determination of the two erythrocyte parameters. Results: Whereas methaemoglobin concentrations in the three erythrocyte genotypes was in the order: HbAS0.05) in methaemoglobin concentration and NADH-methaemoglobin reductase activity between HbAA and HbAS erythrocytes.Conclusion: The results showed a relationship between erythrocyte NADH-methaemoglobin reductase activity and methaemoglobin concentration.
منابع مشابه
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...
متن کاملMethaemoglobin 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...
متن کاملMechanism 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...
متن کاملThe 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.
متن کاملThe reduction of methaemoglobin by ascorbic acid.
In idiopathic methaemoglobinaemia, of which we have investigated'some cases, the occurrence of an atypical form of methaemoglobin' abnormally resistant to reduction has been postulated by Lian, Frumusan & Sassier [1939] as an aetiological factor. It thus became of interest to examine the evidence which has been put forward by Vestling [1942] against the unitary view of methaemoglobin. This auth...
متن کاملStructure of human erythrocyte NADH-cytochrome b5 reductase.
Erythrocyte NADH-cytochrome b(5) reductase reduces methaemoglobin to functional haemoglobin. In order to examine the function of the enzyme, the structure of NADH-cytochrome b(5) reductase from human erythrocytes has been determined and refined by X-ray crystallography. At 1.75 A resolution, the root-mean-square deviations (r.m.s.d.) from standard bond lengths and angles are 0.006 A and 1.03 de...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 2 شماره None
صفحات 1- 6
تاریخ انتشار 2009-10
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023