scholarly journals THE PROLYTIC LOSS OF K FROM HUMAN RED CELLS

1947 ◽  
Vol 30 (3) ◽  
pp. 235-246 ◽  
Author(s):  
Eric Ponder
Keyword(s):  
Serum Albumin ◽  
Individual Cell ◽  
Sodium Taurocholate ◽  
Steady States ◽  
Red Cells ◽  
Red Cell ◽  
Sodium Tetradecyl Sulfate ◽  
The Individual ◽  
Shape Changes ◽  
Human Red Cells

The prolytic loss of K., i.e. the loss of K which takes place from red cells exposed to hypolytic concentrations of lysins, has been measured in systems containing distearyl lecithin, sodium taurocholate, sodium tetradecyl sulfate, saponin, and digitonin, by means of the flame photometer. The lysins are added in various concentrations to washed red cells from heparinized human blood, and the K in the supernatant fluids is determined after various intervals of time and at various temperatures. The prolytic loss Kp is compared in every experiment with the loss Ks into standard systems containing isotonic NaCl alone, with no lysin. The losses Ks and Kp increase with time, so that new steady states are approached logarithmically. The values of Kp which correspond to the new steady states depend on the lysin used, being greatest with taurocholate and smallest with digitonin. The temperature coefficient of the loss is positive, and the extent and course of the losses have no apparent relation to the prolytic shape changes. In systems in which the loss of K is appreciable, it can be inhibited by the addition of plasma or of either cholesterol or serum albumin. Of these two substances, even when used in quantities which have an approximately equal effect in inhibiting hemolysis, serum albumin is much the more effective. Just as the prolytic loss of K occurs without the loss of any Hb, so in concentrations of lysin sufficient to produce hemolysis the loss of K, expressed as a percentage of the total red cell K, increases much more rapidly with lysin concentration than does the loss of Hb expressed as a percentage of the total Hb. The explanation of these relations depends on whether the loss of K is treated as being all-or-none in the case of the individual cell or as being the result of the loss of part of the K from all of the cells. This point has still to be decided.

Shape and Shape Transformation of Heated Human Red Cells

1949 ◽  
Vol 26 (1) ◽  
pp. 35-45
Author(s):  
ERIC PONDER
Keyword(s):  
Serum Albumin ◽  
Red Cells ◽  
Red Cell ◽  
Shape Transformation ◽  
Shape Transformations ◽  
Higher Temperature ◽  
Shape Changes ◽  
Human Red Cells

This paper describes the shape changes and shape transformations observed in human red cells heated for 2 min. to 48, 50 and 52° C. The first change observed is an irregularity of the cell; this is followed by sphering, but the spherical forms can be turned into irregularly shaped disks again by the addition of serum albumin. The sphering is accordingly part of a reversible disk-sphere transformation due to the loss of a (recoverable) anti-sphering substance from the cells. At a slightly higher temperature 50°C.) fragmentation of the cells occurs with the production of fragments which are also capable of undergoing something equivalent to a disk-sphere transformation. The properties upon which the shape transformations depend are therefore not necessarily dependent on the integrity of the red cell as a unit. The fragments derived from the cell may be unequally haemoglobinized, and the Hb is usually lost in a step-wise, as opposed to an all-or-none, manner. Taken together with the loss of anti-sphering substance and an accompanying loss of potassium from the cells, the shape changes preceding fragmentation and the step-wise loss of Hb suggest that the phenomena observed in the heated red cell are part of a process of disintegration of a plastic Hb-bearing ‘solid’.

scholarly journals K-Na EXCHANGE ACCOMPANYING THE PROLYTIC LOSS OF K FROM HUMAN RED CELLS

1947 ◽  
Vol 30 (5) ◽  
pp. 379-387 ◽  
Author(s):  
Eric Ponder
Keyword(s):  
Steady State ◽  
Cell Metabolism ◽  
Ionic Composition ◽  
Surface Membrane ◽  
Sodium Taurocholate ◽  
Red Cells ◽  
Red Cell ◽  
Membrane Changes ◽  
Kinetics Of ◽  
Human Red Cells

In systems containing human red cells and sodium taurocholate as a lysin, or distearyl lecithin as a sphering agent, the prolytic loss of K at 25°C. is accompanied by a gain of Na by the cell, the gain being somewhat greater than the K loss. A small volume increase accompanies the exchange. The kinetics of the K loss and the Na gain are similar to those already described; i.e., the changes are rapid at first, and slow down so that after 12 to 20 hours it appears that a new steady state is being approached. Similar, but smaller, losses of K and gains of Na occur when the cells stand in isotonic NaCl at 25°C. without the addition of a lysin or sphering agent. On these and other experimental grounds, it is impossible to retain the idea that the mammalian red cell in general is impermeable to cations. The cells nevertheless seem to be in a steady state with respect to their environment, their ionic composition changing as the composition of the environment is changed. The possible processes by means of which one steady state can be exchanged for another—changes in the permeability of a surface membrane, changes in the velocity of an active ion transfer process dependent on red cell metabolism, and changes in the activity of the ions in the red cell interior as a result of changes in an orderly internal structure—are discussed.

scholarly journals Kinetics and stoichiometry of Na-dependent Li transport in human red blood cells.

1978 ◽  
Vol 72 (2) ◽  
pp. 249-265 ◽  
Author(s):  
B Sarkadi ◽  
J K Alifimoff ◽  
R B Gunn ◽  
D C Tosteson
Keyword(s):  
Transport System ◽  
Red Cells ◽  
Normal Male ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Human Red Blood Cells ◽  
Na Efflux ◽  
Tightly Coupled ◽  
Male Subjects ◽  
Human Red Cells

This paper describes the kinetics and stoichiometry of a tightly coupled Na-Li exchange transport system in human red cells. The system is inhibited by phloretin and furosemide but not by ouabain. Li influx by this system increases and saturates with increasing concentrations of external Li and internal Na and is inhibited competitively by external Na. Comparable functions relate Li efflux and Na efflux to internal and external Li and Na concentrations. Analysis of these relations yields the following values for the ion concentrations required to half-maximally activate the transport system: internal Na and Li 9.0 and 0.5 mM, respectively, external Na and Li 25 and 1.5 mM, respectively. The system performs a 1:1 exchange of Na and Li moving in opposite directions across the red cell membrane. We found no evidence for a simultaneous transport of more than one Na and Li by the system. The maximum transport rate of Na-dependent Li transport varied between 0.1 and 0.37 mmol/(liter of cells X h) in the red cells of the five normal male subjects studied. No significant variations between individual subjects were observed for bicarbonate-stimulated Li transport and for the residual Li fluxes which occur in the absence of bicarbonate and in the presence of ouabain plus phloretin.

Acetylcholinesterase in Human Erythroid Cells

1973 ◽  
Vol 12 (3) ◽  
pp. 911-923
Author(s):  
R. J. SKAER
Keyword(s):  
Endoplasmic Reticulum ◽  
Nervous System ◽  
Golgi Apparatus ◽  
Red Cells ◽  
The Other ◽  
Red Cell ◽  
Erythroid Cells ◽  
Cell Replacement ◽  
Kinetics Of ◽  
Human Red Cells

Acetylcholinesterase is present in human red cells but cannot be demonstrated by the copper thiocholine test. The enzyme is revealed, however, in the perinuclear cisterna, endoplasmic reticulum and Golgi apparatus of red cell precursors. It is suggested that 2 forms of the enzyme are present, one of which can be demonstrated by the copper thiocholine test, the other cannot; one form may be the precursor of the other. These observations may cast light on the kinetics of red cell replacement and on the interpretation of the results from the copper thiocholine test on other tissues such as the nervous system.

Circulating and tissue hematocrits of normal unanesthetized mice

1959 ◽  
Vol 196 (2) ◽  
pp. 420-422 ◽  
Author(s):  
Julius J. Friedman
Keyword(s):  
Serum Albumin ◽  
Cell Volume ◽  
Plasma Volume ◽  
Venous Blood ◽  
Red Cells ◽  
Red Cell ◽  
Volume Data ◽  
Red Cell Volume ◽  
Volume Measurements ◽  
Total Body

The circulating and tissue hematocrits of normal unanesthetized mice were determined by means of independent red cell and plasma volume measurements. The red cell volume-indicator which was used in this study was radioiron (Fe59) tagged red cells. The plasma volume data were derived by means of radioiodine (I131) labeled serum albumin and were reported earlier (Friedman, Proc. Soc. Exper. Biol. & Med. 88: 323, 1955). The hematocrits of the various tissues were found to be: for spleen 51.3, lung 47.9, muscle 49.9, liver 38.9, intestine, 32.2, skin 29.2 and kidney 24.0%. The total body hematocrit was 35.4% as compared to 48.4 for venous blood. All tissues, with the exception of spleen and lung, contained hematocrits which were lower than that of venous blood suggesting the presence of some mechanism within the various tissues which is capable of effectively separating plasma from red cells.

Biological Activity of a Semisynthetic Flavonoid, O-(β-Hydroxyethyl)rutoside: Light-Scattering and Metabolic Studies of Human Red Cells and Platelets

1973 ◽  
Vol 19 (1) ◽  
pp. 31-35 ◽  
Author(s):  
J W ten Cate ◽  
N J van Haeringen ◽  
J Gerritsen ◽  
E Glasius
Keyword(s):  
Biological Activity ◽  
Light Scattering ◽  
Platelet Aggregation ◽  
Cell Aggregation ◽  
Red Cells ◽  
Red Cell ◽  
High Concentrations ◽  
Platelet Functions ◽  
Human Red Cells ◽  
Red Cell Aggregation

Abstract The effect of O-(β-hydroxyethyl)-rutoside (HR) on human erythrocyte and platelet functions is reported. Only high concentrations of the compound distinctly inhibited red cell and platelet aggregation induced by ADP and epinephrine. Lower concentrations of HR inhibit [14C8]adenosine incorporation into red cells as well as into platelets. Inhibition occurs at both 0°C and 37°C, presumably because diffusion of [14C8]adenosine is hindered. Phosphorylation of [14C8] adenosine by the platelets is not inhibited by HR. The inhibition of red cell aggregation is reversed by washing the cells with plasma. Collectively, these findings indicate an effect of the compound at the site of the membrane, independent of cellular metabolism

scholarly journals Effects Produced by Trypsin on Certain Properties of the Human Red Cell

Blood ◽  
1951 ◽  
Vol 6 (4) ◽  
pp. 350-356 ◽  
Author(s):  
ERIC PONDER
Keyword(s):  
Cell Surface ◽  
Electrophoretic Mobility ◽  
Red Cells ◽  
Red Cell ◽  
Surface Ultrastructure ◽  
Related Enzyme ◽  
Protein Components ◽  
Human Red Cells

Abstract Human red cells treated with trypsin in such a way as to become agglutinable in the presence of incomplete antibodies are affected in certain other respects. Their volume is slightly increased, their ghosts are unusually rigid or "volume-occupying," their osmotic and mechanical fragilities are slightly increased and their electrophoretic mobility is reduced. These changes are probably due to effects on the protein components of the red cell surface ultrastructure. Similar effects are also produced by the related enzyme mexacain.

Blood-perfused working isolated rat heart

1976 ◽  
Vol 41 (4) ◽  
pp. 603-607 ◽  
Author(s):  
M. A. Duvelleroy ◽  
M. Duruble ◽  
J. L. Martin ◽  
B. Teisseire ◽  
J. Droulez ◽  
...  
Keyword(s):  
Rat Heart ◽  
Coronary Flow ◽  
Myocardial Oxygen Consumption ◽  
Isolated Rat Heart ◽  
Red Cells ◽  
Red Cell ◽  
External Work ◽  
Bicarbonate Buffer ◽  
Isolated Rat ◽  
Human Red Cells

We describe a method for perfusion of a working isolated rat heart with washed erythrocytes suspended in a Krebs-Henseleit bicarbonate buffer containing bovine albumin (fraction V). With washed pig red cells, as hematocritwas varied between 0 and 40%, coronary flow (CF), aortic flow (AF), external work (W), and myocardial oxygen consumption (MVO2) were measured. Hemodynamic data at a hematocrit of 30% (CF = 5.4 +/- 0.7 ml/min per g, AF = 75 +/- 8 ml/min per g) were identical with those reported for the intact animal.Coronary sinus PO2 was highest with a red cell-free perfusate suggesting that coronary flow is partially shunted. Human red cells obtained from bankedblood, were tried also with success. With careful filtration, the preparation is stable for 2 h and well suited for study of the dynamics of myocardial oxygen delivery.

Tr: A Canine Red Cell Antigen Related to the A-antigen of Human Red Cells

Vox Sanguinis ◽  
1971 ◽  
Vol 20 (6) ◽  
pp. 542-554
Author(s):  
A.J. Bowdler ◽  
R.W. Bull ◽  
R. Slating ◽  
S.N. Swisher
Keyword(s):  
Red Cells ◽  
Red Cell ◽  
Cell Antigen ◽  
Human Red Cells

Estradiol transport by human red cells

1960 ◽  
Vol 15 (3) ◽  
pp. 515-519 ◽  
Author(s):  
Fritz Bischoff ◽  
George Bryson
Keyword(s):  
Water Solubility ◽  
Intact Cell ◽  
Red Cells ◽  
Red Cell ◽  
Cell Penetration ◽  
Hemoglobin Content ◽  
Hemoglobin Solution ◽  
Low Concentration ◽  
Cell Affinity ◽  
Human Red Cells

Experiments were designed to establish whether the estrogens penetrate the membrane of the red cells or are transported by it. By hemolyzing red cells and reconditioning the ghosts, it was shown that the enzyme, estronase, follows the hemoglobin and therefore indicates that estrone and estradiol penetrate the membrane. Distribution of estradiol between intact red cells or reconditioned ghosts and ghost-free hemolysates of red cells or crystallized hemoglobin solution was proportional to the hemoglobin content when a correction for water solubility was made. Since the ghosts had frac13 the attraction of the intact cell, penetration is required to account for the distribution in the intact cell. Red cell ghost concentrates when prepared under certain conditions were found to have considerable affinity for estradiol, but on the basis of their low concentration per cell could account for only a fraction of the red cell affinity instrumental for estrogen orientation, even if their behavior did not reflect a change in properties during preparation. Ghosts prepared under the mildest conditions failed to demonstrate this affinity for estradiol. Submitted on September 14, 1959

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