Modelling Whole Blood Oxygen Equilibrium: Comparison of Nine Different Models Fitted to Normal Human Data

1985 ◽  
pp. 505-522 ◽  
Author(s):  
J. F. O’Riordan ◽  
T. K. Goldstick ◽  
L. N. Vida ◽  
G. R. Honig ◽  
J. T. Ernest
Keyword(s):  
Whole Blood ◽  
Blood Oxygen ◽  
Oxygen Equilibrium ◽  
Human Data ◽  
Normal Human

scholarly journals Regulation of Blood Oxygen Affinity in the Australian Blackfish Gadopsis Marmoratus: II. Thermal Acclimation

1982 ◽  
Vol 99 (1) ◽  
pp. 245-254
Author(s):  
G. P. DOBSON ◽  
J. BALDWIN
Keyword(s):  
Whole Blood ◽  
Haemoglobin Concentration ◽  
Oxygen Affinity ◽  
Thermal Acclimation ◽  
Acclimation Temperature ◽  
Blood Oxygen ◽  
Molar Ratios ◽  
Oxygen Equilibrium ◽  
Nucleoside Triphosphates ◽  
Blood Oxygen Affinity

1. The effects of thermal acclimation on whole blood oxygen affinity were examined in the freshwater blackfish Gadopsis marmoratus. 2. Oxygen equilibrium curves for 20°C-acclimated fish were shifted to the right of curves obtained for 10°C-acclimated fish when determined at both 20°C and 10°C. Oxygen equilibrium curves obtained for solutions of stripped haemoglobin prepared from blood of 20°C- and 10°C-acclimated fish did not show the differences observed for whole blood. 3. Thermal acclimation did not alter the number, migration rates, or relative amounts of the five electrophoretic forms of haemoglobin present in blackfish blood. 4. The intraerythrocytic concentration of nucleoside triphosphates was higher in the 20°C-acclimated fish than in 10°C-acclimated fish, while the whole blood haemoglobin concentration was lower in the 20 °C-acclimated fish. These differences gave NTP: Hb4 molar ratios of 1.68 for the 20°C-acclimated fish and 1.32 for 10°C-acclimated fish. The effects of nucleoside triphosphates on oxygen affinity were similar for stripped haemoglobins of both acclimation groups. 5. The change in NTP:Hb4 molar ratios with acclimation temperature acts to enhance oxygen unloading to the tissues rather than oxygen uptake at the gills at the higher acclimation temperature. As the waters inhabited by the blackfish retain high oxygen tensions at 20°C, these changes in blood oxygen affinity could be considered adaptive if they were associated with elevated rates of oxygen-dependent metabolism at the higher temperatures.

scholarly journals Oxygen equilibrium curve of normal human blood and its evaluation by Adair's equation.

1977 ◽  
Vol 252 (7) ◽  
pp. 2331-2337 ◽  
Author(s):  
R M Winslow ◽  
M L Swenberg ◽  
R L Berger ◽  
R I Shrager ◽  
M Luzzana ◽  
...  
Keyword(s):  
Human Blood ◽  
Equilibrium Curve ◽  
Oxygen Equilibrium ◽  
Normal Human ◽  
Oxygen Equilibrium Curve ◽  
Normal Human Blood

scholarly journals Rapid method for isolation of normal human peripheral blood eosinophils on discontinuous Percoll gradients and comparison with neutrophils

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 433-440
Author(s):  
RL Roberts ◽  
JI Gallin
Keyword(s):  
Whole Blood ◽  
Cell Layer ◽  
Human Peripheral Blood ◽  
Gradient Centrifugation ◽  
Nitroblue Tetrazolium ◽  
Blood Eosinophil ◽  
Quiescent State ◽  
Simple Method ◽  
Normal Individuals ◽  
Normal Human

Previous studies on human eosinophils often have used cells from patients with hypereosinophilia syndrome or parasitosis owing to the difficulty in isolating pure populations of eosinophils from normal individuals. In the present study, human eosinophils were isolated with a purity of 97%, with 70% recovery from normal individuals with blood eosinophil counts of less than 3%. Human eosinophils are denser than neutrophils, but the range of densities of the two cell types overlap, making purification of eosinophils by density-gradient centrifugation difficult. However, if neutrophils were exposed to the chemotactic peptide (f-Met-Leu-Phe), which did not stimulate eosinophils, the neutrophils' density decreased, shifting them away from the density of eosinophils. Whole normal blood anticoagulated with EDTA was incubated at 37 degrees C for 15 minutes with 10(-6) mol/L f-Met-Leu-Phe and then layered over a discontinuous Percoll gradient (65% and 75% in diluted phosphate-buffered saline) and centrifuged at 400 g for 25 minutes at 22 degrees C. The cell layer between the 65% and 75% Percoll was collected and washed, and hypotonic lysis was used to remove erythrocytes. This cell layer contained 97.3 +/- 0.7% eosinophils (N = 8) with a yield of 4.9 X 10(4) eosinophils per milliliter of whole blood, or 70% of the total eosinophil count. The isolated eosinophils were in a quiescent state but responded to Escherichia coli endotoxin- activated serum with shape change and chemotaxis, membrane depolarization, and reduced nitroblue tetrazolium (96.0 +/- 1.0%), when stimulated with phorbol myristate acetate. In phagocytic assays, 89.3 +/- 1.3% of the eosinophils ingested Candida albicans v 96.0% +/- 1.0% of neutrophils. In contrast, the eosinophils did not respond chemotactically, alter membrane potential, or reduce nitroblue tetrazolium when treated with f-Met-Leu-Phe, and studies with f-Met-Leu- [3H]Phe showed that normal eosinophils lacked expression of receptors for f-Met-Leu-Phe. In control studies, normal eosinophils that were not exposed to f-Met-Leu-Phe during purification also failed to respond to f-Met-Leu-Phe, indicating intrinsic differences between normal eosinophils and neutrophils. Thus, exposure of whole blood to f-Met-Leu- Phe, followed by separation on Percoll is a simple method for rapid isolation of normal human eosinophils.

scholarly journals Rapid method for isolation of normal human peripheral blood eosinophils on discontinuous Percoll gradients and comparison with neutrophils

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 433-440 ◽  
Author(s):  
RL Roberts ◽  
JI Gallin
Keyword(s):  
Whole Blood ◽  
Cell Layer ◽  
Human Peripheral Blood ◽  
Gradient Centrifugation ◽  
Nitroblue Tetrazolium ◽  
Blood Eosinophil ◽  
Quiescent State ◽  
Simple Method ◽  
Normal Individuals ◽  
Normal Human

Abstract Previous studies on human eosinophils often have used cells from patients with hypereosinophilia syndrome or parasitosis owing to the difficulty in isolating pure populations of eosinophils from normal individuals. In the present study, human eosinophils were isolated with a purity of 97%, with 70% recovery from normal individuals with blood eosinophil counts of less than 3%. Human eosinophils are denser than neutrophils, but the range of densities of the two cell types overlap, making purification of eosinophils by density-gradient centrifugation difficult. However, if neutrophils were exposed to the chemotactic peptide (f-Met-Leu-Phe), which did not stimulate eosinophils, the neutrophils' density decreased, shifting them away from the density of eosinophils. Whole normal blood anticoagulated with EDTA was incubated at 37 degrees C for 15 minutes with 10(-6) mol/L f-Met-Leu-Phe and then layered over a discontinuous Percoll gradient (65% and 75% in diluted phosphate-buffered saline) and centrifuged at 400 g for 25 minutes at 22 degrees C. The cell layer between the 65% and 75% Percoll was collected and washed, and hypotonic lysis was used to remove erythrocytes. This cell layer contained 97.3 +/- 0.7% eosinophils (N = 8) with a yield of 4.9 X 10(4) eosinophils per milliliter of whole blood, or 70% of the total eosinophil count. The isolated eosinophils were in a quiescent state but responded to Escherichia coli endotoxin- activated serum with shape change and chemotaxis, membrane depolarization, and reduced nitroblue tetrazolium (96.0 +/- 1.0%), when stimulated with phorbol myristate acetate. In phagocytic assays, 89.3 +/- 1.3% of the eosinophils ingested Candida albicans v 96.0% +/- 1.0% of neutrophils. In contrast, the eosinophils did not respond chemotactically, alter membrane potential, or reduce nitroblue tetrazolium when treated with f-Met-Leu-Phe, and studies with f-Met-Leu- [3H]Phe showed that normal eosinophils lacked expression of receptors for f-Met-Leu-Phe. In control studies, normal eosinophils that were not exposed to f-Met-Leu-Phe during purification also failed to respond to f-Met-Leu-Phe, indicating intrinsic differences between normal eosinophils and neutrophils. Thus, exposure of whole blood to f-Met-Leu- Phe, followed by separation on Percoll is a simple method for rapid isolation of normal human eosinophils.

scholarly journals Diadenosine 5',5'''-p1,p4-tetraphosphate deficiency in blood platelets of the Chediak-Higashi syndrome

Blood ◽  
1985 ◽  
Vol 66 (3) ◽  
pp. 735-737 ◽  
Author(s):  
BK Kim ◽  
FC Chao ◽  
R Leavitt ◽  
AS Fauci ◽  
KM Meyers ◽  
...  
Keyword(s):  
Whole Blood ◽  
Marked Decrease ◽  
Blood Platelets ◽  
Human Platelets ◽  
Dense Granule ◽  
Atp Level ◽  
Dense Granules ◽  
Moderate Reduction ◽  
Normal Human ◽  
Chediak Higashi Syndrome

Abstract Diadenosine tetraphosphate (AP4A) is an unusual nucleotide found in a variety of cells, including platelets. It has been suggested that platelet AP4A is stored in the dense granules and is metabolically inactive. We have studied the AP4A content of blood platelets in two patients and three cattle with Chediak-Higashi syndrome (CHS), a hereditary platelet defect with dense granule deficiency. Acid-soluble extractions of whole blood and platelets were neutralized. The adenosine triphosphate (ATP) level was measured by luminescence technique. To measure the AP4A content, the neutralized extract was treated with phosphomonoesterase for removal of ATP. The AP4A content was then measured by coupling the phosphodiesterase and luciferase reaction. The AP4A content was 0.43 nmol/mg protein for normal human platelets and 0.004 nmol/mg protein for CHS platelets. The ATP/AP4A ratio was 67 for normal and 3,023 for CHS platelets. The whole blood AP4A was reduced by 89% in CHS patients who had only a slight decrease in ATP level (26% reduction). Similarly, bovine platelets with CHS showed a marked decrease of AP4A content and a moderate reduction of the ATP level. The platelet ATP/AP4A ratio was 351 and 3,133 for normal and CHS cattle, respectively. Results demonstrate a marked reduction of AP4A in CHS platelets and suggest that AP4A may be a useful marker for the measurement of dense granule content in platelets.

Whole blood filterability and blood oxygen transport in human hypertension

2016 ◽  
Vol 3 (4) ◽  
pp. 367-373 ◽  
Author(s):  
J. Freitas ◽  
J. Braz-Nogueira ◽  
J. Nogueira da Costa ◽  
J. Martins e Silva
Keyword(s):  
Oxygen Transport ◽  
Whole Blood ◽  
Blood Oxygen ◽  
Human Hypertension ◽  
Blood Filterability

scholarly journals Brief Report: Vitamin B12 and Folate Activity in Normal Human Platelets

Blood ◽  
1968 ◽  
Vol 31 (2) ◽  
pp. 258-262 ◽  
Author(s):  
HARVEY J. WEISS ◽  
ALAN KELLY ◽  
VICTOR HERBERT
Keyword(s):  
Platelet Count ◽  
Vitamin B12 ◽  
Whole Blood ◽  
Human Platelets ◽  
Red Cells ◽  
Red Cell ◽  
Normal Human

Abstract The vitamin B12 and folate content of human platelets have been determined. The B12 concentration was sixfold that in red cells and one-sixth that in leukocytes. In normal whole blood, with a platelet count of 300,000 per cu. mm., the B12 activity contributed by platelets would be 6-21 pg. per ml. The contribution of platelets to the folate activity of normal whole blood averaged 0.4-1.7 ng. per ml. The folate activity in platelets was one-fifth that in an equal volume of red cells, but unlike red cell folate, was not increased by incubating platelet extracts with plasma.

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