Density Increase and Ageing of Erythrocytes in Stored Blood

1989 ◽  
Vol 17 (5) ◽  
pp. 461-466 ◽  
Author(s):  
M. Rocchigiani ◽  
M. Pescaglini ◽  
S. Sestini ◽  
V. Micheli ◽  
C. Ricci
Keyword(s):  
Dehydrogenase Activity ◽  
Whole Blood ◽  
Storage Time ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Acid Citrate Dextrose ◽  
Citrate Dextrose ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Stored Blood ◽  
Citrate Phosphate

An increase in the density of erythrocytes was observed after storage of whole blood for 30 days at 4°C in either acid citrate – dextrose or citrate – phosphate – dextrose – adrenaline. Glucose- 6-phosphate dehydrogenase activity in unfractionated red blood cell lysates did not vary with the storage time. Enzyme activity in the lighter fraction separated by density gradient centrifugation was higher than that in heavier fractions. The decline in glucose-6-phosphate dehydrogenase activity with density was less marked after storage of whole blood for 30 days. It is suggested that density modifications are not related to the ageing of erythrocytes and additional mechanisms may be involved.

scholarly journals Peroxisomal localization of glucose-6-phosphate dehydrogenase and pyrophosphate-stimulated dihydroxyacetone-phosphate acyltransferase in mouse kidney

1987 ◽  
Vol 244 (2) ◽  
pp. 443-448 ◽  
Author(s):  
B N Patel ◽  
M I Mackness ◽  
M J Connock
Keyword(s):  
Subcellular Localization ◽  
Dehydrogenase Activity ◽  
Inorganic Phosphate ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Mouse Kidney ◽  
Dihydroxyacetone Phosphate ◽  
Ph Optimum ◽  
Dependent Activity ◽  
Glucose 6 Phosphate Dehydrogenase

1. The subcellular localization of dihydroxyacetone-phosphate acyltransferase (DHAPAT) (assayed in the presence of pyrophosphate) and glucose-6-phosphate dehydrogenase (NADP+-dependent) activity in mouse kidney was investigated by density-gradient centrifugation. 2. DHAPAT has a predominantly peroxisomal distribution, and the activity in purified peroxisomes is stimulated by various organic and inorganic phosphate-containing compounds. The pH optimum is acid. 3. Approx. 10% of the cellular NADP+-dependent glucose-6-phosphate dehydrogenase activity is associated with peroxisomal fractions and may provide a source of NADPH for the peroxisomal reduction of acyl-dihydroxyacetone phosphate formed by DHAPAT activity.

scholarly journals Effects of Anticoagulants and Storage on Granulocyte Function in Bank Blood

Blood ◽  
1974 ◽  
Vol 43 (2) ◽  
pp. 207-217 ◽  
Author(s):  
Jeffrey McCullough ◽  
Sandra J. Carter ◽  
Paul G. Quie
Keyword(s):  
Whole Blood ◽  
Normal Function ◽  
Bactericidal Assay ◽  
Acid Citrate Dextrose ◽  
Citrate Dextrose ◽  
Granulocyte Function ◽  
And Storage ◽  
Citrate Phosphate ◽  
Bank Blood

Abstract Storage of granulocytes for transfusion has not been practical because it has been considered that granulocyte function in bank blood is retained for only a few hours after collection. In the present study, granulocyte function was evaluated using the bactericidal assay and the quantitative nitroblue tetrazolium (NBT) method. Granulocytes from whole blood collected into acid citrate dextrose (ACD), citrate phosphate dextrose (CPD), heparin, ion exchange, and sodium citrate anticoagulants showed no functional impairment after 24 hr of storage at 4°C. With further storage, all granulocytes showed a loss of NBT activity. However, after 48 and 72 hr, granulocytes from whole blood stored in ACD and CPD killed the expected number of bacteria in the bactericidal assay. Thus, when tested in vitro, granulocytes maintain normal function, at least during the first 24 hr after collection when stored in certain anticoagulants under standard blood bank conditions.

Preparation of optically clear lyophilized human serum for use in preparing control material.

1976 ◽  
Vol 22 (4) ◽  
pp. 456-460 ◽  
Author(s):  
G J Proksch ◽  
D P Bonderman
Keyword(s):  
Human Serum ◽  
Dextran Sulfate ◽  
Raw Materials ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Quality Control Material ◽  
Control Material ◽  
Acid Citrate Dextrose ◽  
Citrate Dextrose ◽  
Citrate Phosphate

Abstract We describe a simple, rapid process--which includes the specific precipitation of pre-beta and beta-lipoproteins with dextran sulfate and divalent metal ions--for preparing an optically clear human serum that retains its clarity upon reconstitution with water after having been frozen and lyophilized. Such serum contains the normal constituents of human serum, except for the removed lipoproteins. The process causes no apparent interference with results of analyses for 22 of the more commonly measured constituents. Fresh or aged pooled serum or blood-bank plasma containing acid-citrate-dextrose or citrate-phosphate-dextrose are equally suitable as raw materials. This stabilized serum is an excellent matrix for use in preparing standards and quality-control material for assay of components of human serum.

The Effect of Methylprednisolone Sodium Succinate on Erythrocyte and Haemoglobin Function

1980 ◽  
Vol 59 (3) ◽  
pp. 163-168 ◽  
Author(s):  
M. Brada ◽  
L. A. Robinson ◽  
A. J. Bellingham
Keyword(s):  
Whole Blood ◽  
Sodium Succinate ◽  
Oxygen Affinity ◽  
Whole Cells ◽  
Methylprednisolone Sodium Succinate ◽  
Acid Citrate Dextrose ◽  
Citrate Dextrose ◽  
Therapeutic Doses

1. As it has been suggested that the beneficial effect of methylprednisolone in shock is due to its effect on erythrocyte oxygen affinity, we studied its effect on incubated erythrocytes and on haemoglobin solution. 2. Incubation of fresh whole blood anticoagulated with acid/citrate/dextrose with methylprednisolone (7 mmol/l) produced a significant decrease in oxygen affinity, which was not seen with lower concentrations of methylprednisolone. When either acid/citrate/dextrose blood stored for 10 days or fresh heparinized blood was used, no significant increase in the partial pressure of oxygen at 50% haemoglobin saturation (P50) was demonstrated even with methylprednisolone at 7 mmol/l. At the highest concentration achieved in plasma with standard therapeutic doses (56 μmol/l) there was no increase in P50 under all the conditions studied. 3. Methylprednisolone reduced the oxygen affinity of haemoglobin in solution. The reduction in oxygen affinity was less than that produced by 2,3-diphosphoglycerate and more than that of either sodium succinate or sodium chloride. 4. From the results of this study we conclude that the effect observed in whole cells is probably due to a direct effect of methylprednisolone on haemoglobin. To produce a significant decrease of oxygen affinity of whole blood in vitro requires a plasma concentration of methylprednisolone above that obtained in plasma in vivo, with the currently used therapeutic doses.

Studies on a ph related zone phenomenon in erythrocytes

1978 ◽  
Vol 36 (2) ◽  
pp. 296-297
Author(s):  
Alan H. Timme
Keyword(s):  
Alcian Blue ◽  
Room Temperature ◽  
Unit Membrane ◽  
Paired Samples ◽  
Cacodylate Buffer ◽  
Charged Membrane ◽  
Acid Citrate Dextrose ◽  
Citrate Dextrose ◽  
Citrate Phosphate ◽  
Positively Charged

In 1967 Baker reported the occurrence of a zone of dense material adjacent to the inner leaflet of the unit membrane of erythrocytes exposed to buffers with a pH 4.5. It was postulated that this arose because the haemoglobin, positively charged at that pH, was attracted to the negatively charged membrane.In an attempt to elucidate the mechanisms underlying the formation of the zone, fresh human erythrocytes were washed for 15 minutes at room temperature in citrate phosphate buffers in which the pH ranged from 4.0 - 7.4, or in a standard preservative solution, Acid Citrate Dextrose (ACD), pH 5.0. Paired samples were subsequently washed in buffer at pH 7.4 for 10 minutes to assess the possible reversibility of any changes produced. The cells were fixed in 2.5% glutaraldehyde in 0.1 m cacodylate buffer at the same pH as the washing buffer for one hour and then processed in two ways: Some were post-fixed in OSO4, The cells were stained with 0.5 - 1% Alcian Blue 8 G S in cacodylate buffer pH 7.0 for 15 - 30 minutes.

The release of radioactive arachidonate from lipids of red blood cell membranes: properties of membrane and serum enzymatic activities

1988 ◽  
Vol 66 (7) ◽  
pp. 795-801 ◽  
Author(s):  
R. Roy Baker ◽  
Zou Dao Loh
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Cell Membranes ◽  
Gradient Centrifugation ◽  
Red Cells ◽  
Percoll Gradient ◽  
Acid Citrate Dextrose ◽  
Red Blood Cell Membranes ◽  
Endogenous Release ◽  
Citrate Dextrose

The release of [3H]arachidonate from the phospholipids of red blood cell membranes of rats has been studied. Membranes of red cells isolated using acid–citrate–dextrose and differential centrifugation showed an endogenous release of arachidonate at pH 7.4 in the presence of CaCl2. Membranes from red cells isolated using heparin and Percoll gradient centrifugation are better substrates for serum-mediated release of arachidonate. These experiments and results with inhibitors suggest that red blood cell and serum phospholipase A2 activities are responsible for this catabolism that may provide arachidonate for subsequent biosynthesis of eicosanoids.

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