Metabolic activities of sheep erythrocytes. II. Formate metabolism

1962 ◽  
Vol 13 (1) ◽  
pp. 45 ◽  
Author(s):  
RA Leng ◽  
EF Annison
Keyword(s):  
Carbon Dioxide ◽  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Aerobic Oxidation ◽  
Carbon Dioxide Production ◽  
Anaerobic Conditions ◽  
Formate Oxidation ◽  
Metabolic Activities ◽  
Sulphydryl Compounds ◽  
Formate Metabolism

Whole sheep blood, washed erythrocytes, and haemolysates showed only a slight capacity to oxidize 14C-labelled formate, as measured by labelled carbon dioxide production. Considerable oxidation of formate by washed erythrocytes or haemolysates occurred in the presence of systems generating hydrogen peroxide enzymically or non-enzymically under aerobic conditions. In addition, methylene blue was found to stimulate markedly the aerobic oxidation of formate by erythrocytes and haemolysates, the effect being abolished under anaerobic conditions. The stimulatory effects of methylene blue and sulphydryl compounds were additive. Evidence was obtained that the effect of methylene blue was mediated through an enzyme which directly or indirectly gave rise to hydrogen peroxide, formate oxidation being achieved by a hydrogen peroxide-catalase complex. No evidence was obtained of formate incorporation into red cells.

The Relations Between Yolk and White in the Hen'S Egg

1931 ◽  
Vol 8 (3) ◽  
pp. 319-329
Author(s):  
JOSEPH NEEDHAM ◽  
MARJORY STEPHENSON ◽  
DOROTHY MOYLE NEEDHAM
Keyword(s):  
Carbon Dioxide ◽  
Catalytic Activity ◽  
Lactic Acid ◽  
Carbon Dioxide Production ◽  
Energy Output ◽  
Vitelline Membrane ◽  
Aerobic Respiration ◽  
Anaerobic Conditions ◽  
Hen’S Egg

1. The vitelline membrane of the infertile hen's egg exhibits no dehydrase activity. 2. The vitelline membrane has no measurable aerobic respiration in vitro, nor has the yolk of the infertile egg. This confirms the view that the carbon dioxide production of the intact egg is not the result of any true respiration. 3. When incubated anaerobically in vitro, bacteriologically sterile yolk produces consistently small amounts of lactic acid. 4. This glycolysis is not the result of any catalytic activity of the vitelline membrane, but takes place throughout the substance of the yolk. 5. Under similar conditions, bacteriologically sterile yolk produces small amounts of a substance or substances estimatable as ethyl alcohol. 6. If the yolk suspension is bacterially contaminated, however, lactic acid and alcohol are produced in amounts closely similar to those found by earlier workers on this subject. 7. The heat of glycolysis, under anaerobic conditions, calculated from the amounts of lactic acid experimentally found to be formed, is of the same order as (a) the calculated requirement of the vitelline membrane (Straub), and (b) the observed heat production (Langworthy and Barott). Thus even if the vitelline membrane is capable of using energy to do osmotic work, the yolk is only capable of supplying it by means of its glycolytic mechanism if the whole energy output of the whole yolk can be made available for doing work at the membrane.

Metabolic activities of sheep erythrocytes. I. Glycolytic activities

1962 ◽  
Vol 13 (1) ◽  
pp. 31 ◽  
Author(s):  
RA Leng ◽  
EF Annison
Keyword(s):  
Carbon Dioxide ◽  
Methylene Blue ◽  
Lactic Acid ◽  
Oxygen Uptake ◽  
Pentose Phosphate Pathway ◽  
Glucose Oxidation ◽  
Lactic Acid Production ◽  
Pentose Phosphate ◽  
Sheep Erythrocytes ◽  
Metabolic Activities

Sheep erythrocytes, which in most animals are impermeable to glucose, show low glycolytic activities relative to human cells. When 14C-labelled glucose was incubated with erythrocyte suspensions the oxygen uptake was 10.9 ± 1.8 µl/hr/ml of cells (5 replications), and glucose oxidation (measured by recovery of [14C]carbon dioxide) was 0.03 ± 0.007 µmole/hr/ml (5). Addition of methylene blue (0.4 µmole/ ml) increased oxygen uptake to 56 ± 3.5 µl/hr/ml (5) and glucose oxidation to 0.36 ± 0.02 µmole/hr/ml. Lactic acid production was increased from 1 .5 ± 0.06 µmole/hr/ml (7) to 1.7 ± 0.11 µmole/hr/ml (7) in the presence of methylene blue. Comparison of the yields of [14C]carbon dioxide from [1-14C]glucose and uniformly labelled [14C]glucose indicated that when stimulated by methylene blue 80–100% of glycolysis proceeded by the pentose phosphate pathway, but in the unstimulated system the alternative aerobic pathway accounted for only about 15% of total glycolysis.

Carbon dioxide production during cardiopulmonary bypass: pathophysiology, measure and clinical relevance

Perfusion ◽  
2016 ◽  
Vol 32 (1) ◽  
pp. 4-12 ◽  
Author(s):  
Marco Ranucci ◽  
Giovanni Carboni ◽  
Mauro Cotza ◽  
Filip de Somer
Keyword(s):  
Carbon Dioxide ◽  
Lactic Acid ◽  
Cardiopulmonary Bypass ◽  
Present Article ◽  
Oxygen Delivery ◽  
Clinical Relevance ◽  
Carbon Dioxide Production ◽  
Carbon Dioxide Removal ◽  
Anaerobic Conditions ◽  
Routine Monitoring

Carbon dioxide production during cardiopulmonary bypass derives from both the aerobic metabolism and the buffering of lactic acid produced by tissues under anaerobic conditions. Therefore, carbon dioxide removal monitoring is an important measure of the adequacy of perfusion and oxygen delivery. However, routine monitoring of carbon dioxide removal is not widely applied. The present article reviews the main physiological and pathophysiological sources of carbon dioxide, the available techniques to assess carbon dioxide production and removal and the clinically relevant applications of carbon dioxide-related variables as markers of the adequacy of perfusion during cardiopulmonary bypass.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (6) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

RESPIRATION OF STRAIN L CELLS AND OF THEIR VARIANT, LE CELLS

1964 ◽  
Vol 42 (4) ◽  
pp. 513-520 ◽  
Author(s):  
S. Fedoroff ◽  
V. R. Woodford
Keyword(s):  
Carbon Dioxide ◽  
Oxygen Uptake ◽  
Parent Strain ◽  
Carbon Dioxide Production ◽  
Anaerobic Conditions ◽  
L Cells

The oxygen uptake and carbon dioxide production of strain L cells and their variant LE cells were measured by using Warburg techniques with glucose as the sole substrate. The variant LE cells consumed oxygen at a greater rate than did the parent strain L cells. Under anaerobic conditions the situation was reversed, that is, LE cells released less carbon dioxide than did the parent strain L cells.

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