THE PENTOSE PHOSPHATE METABOLIC PATHWAY IN THE HUMAN ERYTHROCYTE: III. THE STABILITY OF THE PENTOSE PHOSPHATE METABOLIC SYSTEM IN PRESERVED ERYTHROCYTES

1961 ◽  
Vol 39 (3) ◽  
pp. 545-550 ◽  
Author(s):  
Y. S. Brownstone ◽  
O. F. Denstedt
Keyword(s):  
Metabolic Pathway ◽  
Human Erythrocyte ◽  
Pentose Phosphate ◽  
Red Cells ◽  
Prolonged Storage ◽  
Metabolic System ◽  
The Stability ◽  
Citrate Dextrose ◽  
Human Red Cells

The activity of the enzymes of the pentose phosphate metabolic pathway in the dialyzed stroma-free hemolyzate (SFH) from human red cells remains unaltered after prolonged storage of the blood in acidified citrate dextrose (ACD) medium at 4 °C.Erythrocytes from children with galactosemia were found to have normal transketolase and transaldolase activity.

THE PENTOSE PHOSPHATE METABOLIC PATHWAY IN THE HUMAN ERYTHROCYTE: II. THE TRANSKETOLASE AND TRANSALDOLASE ACTIVITY OF THE HUMAN ERYTHROCYTE

1961 ◽  
Vol 39 (3) ◽  
pp. 533-543 ◽  
Author(s):  
Y. S. Brownstone ◽  
O. F. Denstedt
Keyword(s):  
Human Erythrocyte ◽  
Soluble Fraction ◽  
Pentose Phosphate ◽  
Ion Concentration ◽  
Thiamine Pyrophosphate ◽  
Magnesium Ions ◽  
Michaelis Constant ◽  
Hydrogen Ion Concentration ◽  
Wide Range ◽  
Human Red Cells

Transketolase, in the human erythrocyte, is confined to the soluble fraction of the cell. The activation energy for the formation of sedoheptulose-7-phosphate (S-7-P) from pentose phosphate was found to be 11,500 calories and the rate of formation of S-7-P to be directly proportional to the concentration of the enzyme. The Michaelis constant, with ribose-5-phosphate (R-5-P) as the added substrate, was found to be 6 × 10−3 M. The activity of the enzyme is close to the maximum over a wide range of hydrogen ion concentration (pH 7.1 to 8.3) with only a gradual decrease beyond these limits. The transketolase, in the dialyzed stroma-free hemolyzate, is active without the addition of magnesium ions or thiamine pyrophosphate. It is unaffected by sulphydryl-binding inhibitors and by EDTA and oxythiamine pyrophosphate.Transaldolase activity also has been demonstrated in the hemolyzate of human red cells. The rate of the production of hexose phosphate from sedoheptulose-7-phosphate was found to be of the order of 40 μmoles/g Hb/hour. The activity of the enzyme is close to the maximum between pH 7.18 and 7.75.

Recovery of Human Red Cells after Prolonged Storage at − 79° C.

Nature ◽  
1952 ◽  
Vol 169 (4311) ◽  
pp. 1013-1014 ◽  
Author(s):  
H. A. SLOVITER
Keyword(s):  
Red Cells ◽  
Prolonged Storage ◽  
Human Red Cells

THE PENTOSE PHOSPHATE METABOLIC PATHWAY IN THE HUMAN ERYTHROCYTE: I. THE TRANSFORMATION OF RIBOSE-5-PHOSPHATE TO KETOPENTOSE-5-PHOSPHATE

1961 ◽  
Vol 39 (3) ◽  
pp. 527-532 ◽  
Author(s):  
Y. S. Brownstone ◽  
O. F. Denstedt
Keyword(s):  
Metabolic Pathway ◽  
Human Erythrocyte ◽  
Pentose Phosphate ◽  
Red Cell

Ribose-5-phosphate is converted to ketopentose-5-phosphate by red cell hemolyzate at the rate of 3.6 mmoles/g Hb/hour at 37 °C. The rate of activity of the enzymes remains fairly steady over a broad range of pH (6.5 to 9.0).

scholarly journals Towards microfluidic-based depletion of stiff and fragile human red cells that accumulate during blood storage

Lab on a Chip ◽  
2015 ◽  
Vol 15 (2) ◽  
pp. 448-458 ◽  
Author(s):  
Sha Huang ◽  
Han Wei Hou ◽  
Tamir Kanias ◽  
Jonas Tadeu Sertorio ◽  
Huichao Chen ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Red Cells ◽  
Prolonged Storage ◽  
Biophysical Properties ◽  
Blood Storage ◽  
Human Red Cells

In this study, the effects of prolonged storage on several biophysical properties of red blood cells (RBCs) were investigated.

In Vitro Assay of Platelet Adhesiveness with Washed and Tanned Human Red Cells

1968 ◽  
Vol 20 (03/04) ◽  
pp. 384-396 ◽  
Author(s):  
G Zbinden ◽  
S Tomlin
Keyword(s):  
Platelet Adhesion ◽  
Sodium Citrate ◽  
Blood Platelets ◽  
In Vitro Assay ◽  
Red Cells ◽  
Platelet Adhesiveness ◽  
Vitro Assay ◽  
In Vitro System ◽  
Human Red Cells

SummaryAn in vitro system is described in which adhesion of blood platelets to washed and tannic acid-treated red cells was assayed quantitatively by microscopic observation. ADP, epinephrine and TAME produced a reversible increase in platelet adhesiveness which was antagonized by AMP. With Evans blue, polyanetholsulfonate, phthalanilide NSC 38280, thrombin and heparin at concentrations above 1-4 u/ml the increase was irreversible. The ADP-induced increase in adhesiveness was inhibited by sodium citrate, EDTA, AMP, ATP and N-ethylmaleimide. EDTA, AMP and the SH-blocker N-ethylmaleimide also reduced spontaneous platelet adhesion to red cells. No significant effects were observed with adenosine, phenprocoumon, 5-HT, phthalanilide NSC 57155, various estrogens, progestogens and fatty acids, acetylsalicylic acid and similarly acting agents, hydroxylamine, glucose and KCN. The method may be useful for the screening of thrombogenic and antithrombotic properties of drugs.

Metabolic control of the K+ channel of human red cells

1990 ◽  
Vol 116 (1) ◽  
pp. 19-29 ◽  
Author(s):  
Pedro J. Romero ◽  
Carlos E. Ortíz ◽  
Carmelo Melitto
Keyword(s):  
Metabolic Control ◽  
Red Cells ◽  
K Channel ◽  
Human Red Cells
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