scholarly journals Efflux of Red Cell Water into Buffered Hypertonic Solutions

1960 ◽  
Vol 43 (4) ◽  
pp. 707-712 ◽  
Author(s):  
Edwin G. Olmstead

Buffered NaCl solutions hypertonic to rabbit serum were prepared and freezing point depressions of each determined after dilution with measured amounts of water. Freezing point depression of these dilutions was a linear function of the amount of water added. One ml. of rabbit red cells was added to each 4 ml. of the hypertonic solutions and after incubation at 38°C. for 30 minutes the mixture was centrifuged and a freezing point depression determined on the supernatant fluid. The amount of water added to the hypertonic solutions by the red cells was calcuated from this freezing point depression. For each decrease in the freezing point of -0.093°C. of the surrounding solution red cells gave up approximately 5 ml. of water per 100 ml. of red cells in the range of -0.560 to -0.930°C. Beyond -0.930°C. the amount of water given up by 100 ml. of red cells fits best a parabolic equation. The maximum of this equation occurred at a freezing point of the hypertonic solution of -2.001°C. at which time the maximum amount of water leaving the red cells would be 39.9 ml. per 100 ml. of red cells. The data suggest that only about 43 per cent of the red cell water is available for exchange into solutions of increasing tonicity.

1960 ◽  
Vol 44 (2) ◽  
pp. 227-233 ◽  
Author(s):  
Edwin G. Olmstead

Rabbit erythrocytes were washed in buffered NaCl solutions isotonic with rabbit serum (Δt -0.558°C.) and suspended in buffered NaCl solutions of tonicity equidistant from intracellular tonicity (Δt = -0.558°C. ± 0.112°C.) of varying pH and incubated at varying temperatures. After incubation, the freezing point depression (Δt) was measured on the supernatant. Change in the Δt measured change in the water content of the extracellular solutions—water being withdrawn by erythrocytes (WI) from the hypotonic solutions and added (WE) to the hypertonic solutions. WE was always less than WI and was inversely proportional to the pH in the range 6.5–8.0. WE was significantly increased by lowering the temperature of the cell suspension to 4°C. WI was increased by raising or lowering the pH or raising the temperature of the cell suspension. WE x WI ≠ k. WE and WI were affected differently by changes in pH and temperature. It was concluded that WE and WE were probably under different physicochemical control.


1978 ◽  
Vol 44 (2) ◽  
pp. 254-257 ◽  
Author(s):  
Y. Kakiuchi ◽  
A. B. DuBois ◽  
D. Gorenberg

Hansen's membrane manometer method for measuring plasma colloid osmotic pressure was used to obtain the osmolality changes of dogs breathing different levels of CO2. Osmotic pressure was converted to osmolality by calibration of the manometer with saline and plasma, using freezing point depression osmometry. The addition of 10 vol% of CO2 to tonometered blood caused about a 2.0 mosmol/kg H2O increase of osmolality, or 1.2% increase of red blood cell volume. The swelling of the red blood cells was probably due to osmosis caused by Cl- exchanged for the HCO3- which was produced rapidly by carbonic anhydrase present in the red blood cells. The change in colloid osmotic pressure accompanying a change in co2 tension was measured on blood obtained from dogs breathing different CO2 mixtures. It was approximately 0.14 mosmol/kg H2O per Torr Pco2. The corresponding change in red cell volume could not be calculated from this because water can exchange between the plasma and tissues.


1959 ◽  
Vol 197 (3) ◽  
pp. 648-652 ◽  
Author(s):  
G. B. Spurr ◽  
George Barlow

Plasma and erythrocyte Na, K, Cl and water have been determined in hyperventilated dogs cooled to 25°C for periods up to 4 hours, in animals heated to either 41.5°C or 42.5°C for 1 hour and in hyperventilated-normothermic dogs. The induced respiratory alkalemia in both normothermic and hypothermic animals appeared to result in a shift of Na from plasma into red cells. Plasma K was reduced in both normothermic and hypothermic dogs, whereas a K elevation in erythrocytes occurred only in the normothermic animals following hyperventilation. Erythrocyte K remained unchanged in hypothermia. It seems, therefore, that the fall in plasma K which occurs in alkalemic normothermic dogs is due partially to a movement of K into red cells whereas, in hypothermia the K leaving extracellular fluid enters cells other than erythrocytes. The plasma and red cell electrolyte changes observed in the two hyperthermic groups of dogs were all in the direction of an increase. It is concluded that these changes were primarily the result of the increased body temperature and of consequent reductions in plasma and red cell water content, rather than the result of the blood pH changes associated with hyperthermia.


1948 ◽  
Vol 87 (4) ◽  
pp. 301-314 ◽  
Author(s):  
George K. Hirst

The influenza virus receptors of fowl red cells and the influenza virus inhibitor of normal rabbit serum have the following attributes in common: They are stable at high temperatures and in solutions of pH as high as 10.0. They both resist destruction by a number of oxidizing agents but are readily destroyed by sodium periodate, trypsin, and influenza virus. These facts suggest that the red cell receptor and the normal serum inhibitor are either the same or analogous substances and that they may belong to the mucoprotein class of compounds.


1930 ◽  
Vol 14 (2) ◽  
pp. 163-177 ◽  
Author(s):  
Harold A. Abramson

A survey of the published electrophoretic mobilities of certain mammalian red cells reveals that the isoelectric points accorded to these cells are the result of equilibria incidental to red cell destruction. The electrophoretic mobilities of normal washed sheep and human cells have now been studied in 0.85 per cent NaCl solutions from about pH 3.6 to 7.4. All measurements were made within 2 minutes of the preparation of the suspension of red cells. In no case was reversal of sign of charge observed under these conditions. Reversal of sign of charge occurred only after sufficient time had elapsed to permit sufficient adsorption of the products of red cell destruction. There is little change in mobility as the pH of the medium is decreased. Reversal of sign of charge does occur in the presence of normal and immune (anti-sheep) rabbit sera. The isoelectric point determined under these conditions does not appear to be connected specifically with the immune body but is perhaps associated with phenomena incidental to red cell destruction and the presence of serum. The characteristic lowering of mobility by amboceptor occurs, however, from pH 4.0 to pH 7.4. The curves of mobility plotted against pH for normal and for immune sera support the viewpoint that the identity of the isoelectric points for normal and sensitized sheep cells is not primarily concerned with the immune reaction. It is most unlikely that an "albumin" or a "globulin" surface covers red cells with a complete protein film. Although serum protein reacts with red cells in acid solutions, this is not demonstrable for gelatin. The lowering of mobility usually ascribed to anti-sheep rabbit serum may also occur, but to a lesser degree, in normal rabbit serum. This diminution of mobility is not, in the first place, associated with sensitization to hemolysis induced by complement. This supports the view that only a very small part of the red cell surface need be changed in order to obtain complete hemolysis in the presence of complement.


1968 ◽  
Vol 52 (5) ◽  
pp. 825-853 ◽  
Author(s):  
C. M. Gary-Bobo ◽  
A. K. Solomon

The present studies are concerned with a detailed examination of the apparent anomalous osmotic behavior of human red cells. Red cell water has been shown to behave simultaneously as solvent water for nonelectrolytes and nonsolvent water, in part, for electrolytes. The nonsolvent properties are based upon assumptions inherent in the conventional van't Hoff equation. However, calculations according to the van't Hoff equation give osmotic volumes considerably in excess of total cell water when the pH is lowered beyond the isoelectric point for hemoglobin; hence the van't Hoff equation is inapplicable for the measurement of the solvent properties of the red cell. Furthermore, in vitro measurements of osmotic and other properties of 3.7 millimolal solutions of hemoglobin have failed to reveal the presence of any salt exclusion. A new hypothesis has been developed from thermodynamic principles alone, which predicts that, at constant pH, the net charge on the hemoglobin molecule decreases with increased hemoglobin concentration. The existence of such cooperative interaction may be inferred from the effect of pH on the changes in hemoglobin net charge as the spacing between the molecules decreases. The resultant movement of counterions across the cell membrane causes the apparent anomalous osmotic behavior. Quantitative agreement has been found between the anion shift predicted by the equation and that observed in response to osmotic gradients. The proposed mechanism appears to be operative in a variety of tissues and could provide an electrical transducer for osmotic signals.


1963 ◽  
Vol 117 (4) ◽  
pp. 647-661 ◽  
Author(s):  
Robert S. Evans ◽  
Margaret Bingham ◽  
Russell S. Weiser

A disease characterized by frequent association of enteritis and polyagglutinable cells often develops in weanling rabbits. The red cell lesion renders the cells susceptible to agglutination and hemolysis in normal rabbit sera. The degree of red cell abnormality varies among different animals and disappears when the animals recover. The abnormality of the red cells responsible for their polyagglutinability and susceptibility to hemolysis was resistant to the action of trypsin or papain and persisted in heated stroma preparations derived from polyagglutinable cells. The factors necessary for agglutination and hemolysis of the polyagglutinable cells are present in normal rabbit sera but are lacking in the sera of affected rabbits. These factors returned to normal levels as the polyagglutinable cell lesion disappeared. The sera of rabbits with polyagglutinable cells contained normal levels of complement and properdin. Whereas the agglutinating factor in normal sera is heat-stable at 56°C for 30 minutes, the hemolytic factor is heat labile. The hemolytic factor is apparently distinct from complement and properdin since it was adsorbed from normal rabbit serum by zymosan or by polyagglutinable cells at 0°C. However, complement was fixed when normal rabbit serum was reacted with stroma from polyagglutinable cells. Hemolysis of polyagglutinable cells by normal rabbit serum at 25°C was inhibited by preliminary incubation of the mixture at 0°C prior to incubation at 25°C. Evidence was obtained which indicated that this inhibition was due to progression of a reaction involving Ca++ independent of a reaction involving Mg++.


1964 ◽  
Vol 47 (3_Suppl) ◽  
pp. S28-S36
Author(s):  
Kailash N. Agarwal
Keyword(s):  

ABSTRACT Red cells were incubated in vitro with sulfhydryl inhibitors and Rhantibody with and without prior incubation with prednisolone-hemisuccinate. These erythrocytes were labelled with Cr51 and P32 and their disappearance in vivo after autotransfusion was measured. Prior incubation with prednisolone-hemisuccinate had no effect on the rate of red cell disappearance. The disappearance of the cells was shown to take place without appreciable intravascular destruction.


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