VI. Methemoglobin Formation in Infantile Erythrocytes

2015 ◽  
pp. 40-44
Keyword(s):  
Methemoglobin Formation

scholarly journals Hemoglobin Oxidation in Stored Blood Accelerates Hemolysis and Oxidative Injury to Red Blood Cells

2020 ◽  
Vol 12 (04) ◽  
pp. 244-249
Author(s):  
Ibrahim Mustafa ◽  
Tameem Ali Qaid Hadwan
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Morphological Changes ◽  
Hemoglobin Concentration ◽  
Red Cell Membrane ◽  
Rbc Membrane ◽  
Hemoglobin Oxidation ◽  
Rbc Indices ◽  
Methemoglobin Formation ◽  
Stored Blood

Abstract Introduction Maintaining blood supply is a challenge in blood banks. Red blood cells (RBCs) stored at 4°C experience issues of biochemical changes due to metabolism of cells, leading to changes collectively referred to as “storage lesions.” Oxidation of the red cell membrane, leading to lysis, contributes to these storage lesions. Methods Blood bags with CPD-SAGM stored at 4°C for 28 days were withdrawn aseptically on days 1, 14, and 28. Hematology analyzer was used to investigate RBC indices. Hemoglobin oxidation was studied through spectrophotometric scan of spectral change. RBC lysis was studied with the help of Drabkin's assay, and morphological changes were observed by light and scan electron microscopy. Results RBCs show progressive changes in morphology echinocytes and spherocytes on day 28. There was 0.85% RBC lysis, an approximately 20% decrease in percentage oxyhemoglobin, and a 14% increase in methemoglobin formation, which shows hemoglobin oxidation on day 28. Conclusions Oxidative damage to RBC, with an increase in storage time was observed in the present study. The observed morphological changes to RBC during the course of increased time shows that there is progressive damage to RBC membrane and a decrease in hemoglobin concentration; percentage RBC lysis is probably due to free hemoglobin and iron.

scholarly journals EVALUATION OF A STROMA-FREE HEMOGLOBIN SOLUTION FOR USE AS A PLASMA EXPANDER

1967 ◽  
Vol 126 (6) ◽  
pp. 1127-1142 ◽  
Author(s):  
S. Frederick Rabiner ◽  
J. Raymond Helbert ◽  
Harry Lopas ◽  
Lila H. Friedman
Keyword(s):  
Carrying Capacity ◽  
Vital Signs ◽  
Free Hemoglobin ◽  
Hemoglobin Solution ◽  
Plasma Expander ◽  
Chronic Effects ◽  
Coagulant Activity ◽  
Methemoglobin Formation ◽  
Oxygen Carrying Capacity ◽  
Acute And Chronic Effects

The preparation of large quantities of a stable, stroma-free hemoglobin solution without coagulant activity is described. Following infusion of this solution into phlebotomized dogs, there is no methemoglobin formation, no adverse effects on vital signs, and no demonstrable activation of blood coagulation. The hemoglobin maintains its oxygen-carrying capacity and liberates oxygen into tissues. Acute and chronic effects on renal function following infusion of this preparation were also studied and no effect on clearance of urea, creatinine, or P.A.H. could be demonstrated. There was no change in urinary output and histological sections revealed no lesions attributable to hemoglobin toxicity. It is concluded that a stroma-free hemoglobin solution may have use as a plasma expander.

Crocin protects human erythrocytes from nitrite-induced methemoglobin formation and oxidative damage

2016 ◽  
Vol 40 (12) ◽  
pp. 1320-1331 ◽  
Author(s):  
Fariheen Aisha Ansari ◽  
Shaikh Nisar Ali ◽  
Riaz Mahmood
Keyword(s):  
Oxidative Damage ◽  
Human Erythrocytes ◽  
Methemoglobin Formation

scholarly journals THE FORMATION OF METHEMOGLOBIN BY STREPTOCOCCUS VIRIDANS

1916 ◽  
Vol 24 (4) ◽  
pp. 315-327 ◽  
Author(s):  
Francis G. Blake
Keyword(s):  
Blood Cells ◽  
Chemical Nature ◽  
Oxidation Process ◽  
Streptococcus Viridans ◽  
Bacterial Cells ◽  
Active Oxidation ◽  
Oxidation Processes ◽  
Reduction Processes ◽  
Methemoglobin Formation ◽  
Metabolic Activities

Cultures of Streptococcus viridans when brought into contact with red blood corpuscles have the power of transforming oxyhemoglobin into methemoglobin. The reaction occurs only in the presence of living streptococci when they are able to carry on their metabolic activities. The intensity of the reaction runs roughly parallel with the period of growth and multiplication of the bacteria and gradually diminishes and disappears as growth ceases. There is no apparent relation between the activity of a given strain of Streptococcus viridans in producing methemoglobin and its source or virulence. If the streptococci are suspended in salt solution they are unable to change oxyhemoglobin into methemoglobin unless some nutrient substance is present. Of the various nutrient substances tested dextrose is the most efficient in enabling the organisms to bring about the reaction. The reaction does not occur in the absence of oxygen, and is retarded by an excess of oxygen. Substances which tend to reduce the metabolic activities of the bacteria to a minimum exert an inhibitory action on methemoglobin formation. While not definitely proving it to be so, the results obtained in the above experiments strongly support the supposition that the reaction is not due to injurious substances produced by the bacteria or to products arising from the decomposition of the nutrient material present, but rather to the metabolic activities of the bacteria themselves when they are surrounded by environmental conditions which render growth and multiplication possible. The exact chemical nature of the change of oxyhemoglobin to methemoglobin is not known, but it is probably an oxidation process or a combination of reduction and oxidation processes, as pointed out by Heubner. As Cole has shown, the action of aminophenol is of great interest in this connection, in that it acts like a catalytic agent in being able to transform much more hemoglobin into methemoglobin than would be possible if the reaction were a simple molecular one. The metabolic activities of bacteria are largely in the nature of oxidation and reduction processes. The transformation of oxyhemoglobin into methemoglobin by streptococci of the viridans type, therefore, may be analogous to the action of such substances as aminophenol, and the reaction may be due to the active oxidation and reduction processes occurring in the neighborhood of the bacterial cells. The failure of the reaction to occur in the absence of oxygen and its retardation in the presence of an excess of oxygen, both with streptococci and with pneumococci (Cole) would seem to support this theory. Such results, however, may be due to the abnormal conditions surrounding the bacteria with consequent inhibition of their metabolic activities. Cole concluded as the result of his study of methemoglobin formation by pneumococci that since bacteria may injure red blood cells apparently by disturbances in oxidation in the immediate neighborhood of the organisms rather than by the production of a definite toxin, it is possible that bacteria may injure other tissue cells in a like manner and that the pathological effects produced by these bacteria may be explained on this basis. The experimental results recorded above have shown that the formation of methemoglobin by Streptococcus viridans in no way differs from its formation by pneumococci, and they lend support to the theory that bacteria may be injurious to tissues because of the disturbances in oxidation brought about by the metabolic activities of the organisms, especially those associated with growth and multiplication. It is believed that this theory may be particularly applicable to the pathological effects caused by Streptococcus vindans because the lesions produced by it, whether single or multiple, both in man and in experimental animals, are prone to be localized and associated with the actual presence of the streptococci in the lesions.

In vitro methemoglobin formation in human blood exposed to NO2

1983 ◽  
Vol 30 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Hugo Chiodi ◽  
Clarence R. Collier ◽  
John G. Mohler
Keyword(s):  
Human Blood ◽  
Methemoglobin Formation

scholarly journals STUDIES ON OXIDATION AND REDUCTION BY PNEUMOCOCCUS

1924 ◽  
Vol 39 (5) ◽  
pp. 757-775 ◽  
Author(s):  
James M. Neill ◽  
Oswald T. Avery
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidation Process ◽  
Degradation Products ◽  
Active Agent ◽  
Reduced Form ◽  
Peroxide Formation ◽  
Sterile Saline ◽  
Cell Extracts ◽  
Oxidation Reduction ◽  
Methemoglobin Formation

1. Sterile broth extracts of unwashed pneumococci actively destroy hemoglobin to methemoglobin and lower degradation products. 2. Sterile saline extracts of washed pneumococci do not by themselves form methemoglobin; extracts of this type may be completed or activated by the addition of certain complementary substances such as meat infusion and yeast extract. 3. The hemoglobin-destroying activity of pneumococcus extract is lost by exposure to 65°C. for 10 minutes. 4. The properties of an extract upon which these blood changes depend are related to other known oxidation-reduction functions of the same extract. 5. Oxyhemoglobin is converted to methemoglobin only by cell extracts in the reduced form; completely oxidized extracts are inactive in the presence of blood. The action of hydrogen peroxide and the influence of blood catalase on these reactions are discussed. 6. During the reaction between oxyhemoglobin and pneumococcus extract oxygen is consumed. 7. The mechanism of methemoglobin formation by pneumococcus is interpreted as an oxidation process in which deoxygenation of oxyhemoglobin and peroxide formation occur as intermediary reactions. The active agent of the oxidation of hemoglobin is considered to be a peroxide of bacterial origin.

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