scholarly journals DONNAN EQUILIBRIUM AND THE PHYSICAL PROPERTIES OF PROTEINS

1921 ◽  
Vol 3 (6) ◽  
pp. 827-841 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
High Viscosity ◽  
Relative Volume ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin ◽  
Low Viscosity ◽  
Donnan Equilibrium ◽  
Protein Ions ◽  
Order Of Magnitude ◽  
The Difference

1. Gelatin solutions have a high viscosity which in the case of freshly prepared solutions varies under the influence of the hydrogen ion concentration in a similar way as the swelling, the osmotic pressure, and the electromotive forces. Solutions of crystalline egg albumin have under the same conditions a comparatively low viscosity which is practically independent of the pH (above 1.0). This difference in the viscosities of solutions of the two proteins seems to be connected with the fact that solutions of gelatin have a tendency to set to a Jelly while solutions of crystalline egg albumin show no such tendency at low temperature and pH above 1.0. 2. The formulæ for viscosity demand that the difference in the order of magnitude of the viscosity of the two proteins should correspond to a difference in the relative volume occupied by equal masses of the two proteins in the same volume of solution. It is generally assumed that these variations of volume of dissolved proteins are due to the hydration of the isolated protein ions, but if this view were correct the influence of pH on viscosity should be the same in the case of solutions of gelatin, of amino-acids, and of crystalline egg albumin, which, however, is not true. 3. Suspensions of powdered gelatin in water were prepared and it was found, first, that the viscosity of these suspensions is a little higher than that of gelatin solutions of the same concentration, second, that the pH influences the viscosity of these suspensions similarly as the viscosity of freshly prepared gelatin solutions, and third, that the volume occupied by the gelatin in the suspension varies similarly as the viscosity which agrees with the theories of viscosity. It is shown that this influence of the pH on the volume occupied by the gelatin granules in suspension is due to the existence of a Donnan equilibrium between the granules and the surrounding solution.

scholarly journals DONNAN EQUILIBRIUM AND THE PHYSICAL PROPERTIES OF PROTEINS

1921 ◽  
Vol 4 (1) ◽  
pp. 73-95 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
High Viscosity ◽  
Relative Volume ◽  
Solid Particles ◽  
Protein Solutions ◽  
Gelatin Solution ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin ◽  
Donnan Equilibrium ◽  
Order Of Magnitude ◽  
Protein Particles

1. The proof is completed that the influence of electrolytes on the viscosity of suspensions of powdered particles of gelatin in water is similar to the influence of electrolytes on the viscosity of solutions of gelatin in water. 2. It has been suggested that the high viscosity of proteins is due to the existence of a different type of viscosity from that existing in crystalloids. It is shown that such an assumption is unnecessary and that the high viscosity of solutions of isoelectric gelatin can be accounted for quantitatively on the assumption that the relative volume of the gelatin in solution is comparatively high. 3. Since isoelectric gelatin is not ionized, the large volume cannot be due to a hydration of gelatin ions. It is suggested that this high volume of gelatin solutions is caused by the existence in the gelatin solution of submicroscopic pieces of solid gelatin occluding water, the relative quantity of which is regulated by the Donnan equilibrium. This would also explain why the influence of electrolytes on the viscosity of gelatin solutions is similar to the influence of electrolytes on the viscosity of suspensions of particles of gelatin. 4. This idea is supported by experiments on solutions and suspensions of casein chloride in which it is shown that their viscosity is chiefly due to the swelling of solid particles of casein, occluding quantities of water regulated by the Donnan equilibrium; and that the breaking up of these solid particles into smaller particles, no longer capable of swelling, diminishes the viscosity. 5. This leads to the idea that proteins form true solutions in water which in certain cases, however, contain, side by side with isolated ions and molecules, submicroscopic solid particles capable of occluding water whereby the relative volume and the viscosity of the solution is considerably increased. This accounts not only for the high order of magnitude of the viscosity of such protein solutions but also for the fact that the viscosity is influenced by electrolytes in a similar way as is the swelling of protein particles. 6. We therefore reach the conclusion that there are two sources for the viscosity of protein solutions; one due to the isolated protein ions and molecules, and the other to the submicroscopic solid particles contained in the solution. The viscosity due to the isolated molecules and ions of proteins we will call the general viscosity since it is of a similar low order of magnitude as that of crystalloids in solution; while the high viscosity due to the submicroscopic solid protein particles capable of occluding water and of swelling we will call the special viscosity of protein solutions. Under ordinary conditions of hydrogen ion concentration and temperature (and in not too high a concentration of the protein in solution) the general viscosity due to isolated ions and molecules prevails in solutions of crystalline egg albumin and in solutions of metal caseinates (where the metal is monovalent) while under the same conditions the second type of viscosity prevails in solutions of gelatin and in solutions of acid-salts of casein; and also in solutions of crystalline egg albumin at a pH below 1.0 and at higher temperatures. The special viscosity is higher in solutions of gelatin than of casein salts for the probable reason that the amount of water occluded by the submicroscopic solid gel particles in a gelatin solution is, as a rule, considerably higher than that occluded by the corresponding particles of casein.

scholarly journals DONNAN EQUILIBRIUM AND THE PHYSICAL PROPERTIES OF PROTEINS

1921 ◽  
Vol 3 (5) ◽  
pp. 667-690 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Osmotic Pressure ◽  
Chloride Solution ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Neutral Salt ◽  
Hydrogen Ion Concentration ◽  
Monovalent Anion ◽  
Donnan Equilibrium ◽  
The Difference ◽  
Fair Degree

1. It is shown that a neutral salt depresses the potential difference which exists at the point of equilibrium between a gelatin chloride solution contained in a collodion bag and an outside aqueous solution (without gelatin). The depressing effect of a neutral salt on the P.D. is similar to the depression of the osmotic pressure of the gelatin chloride solution by the same salt. 2. It is shown that this depression of the P.D. by the salt can be calculated with a fair degree of accuracy on the basis of Nernst's logarithmic formula on the assumption that the P.D. which exists at the point of equilibrium is due to the difference of the hydrogen ion concentration on the opposite sides of the membrane. 3. Since this difference of hydrogen ion concentration on both sides of the membrane is due to Donnan's membrane equilibrium this latter equilibrium must be the cause of the P.D. 4. A definite P.D. exists also between a solid block of gelatin chloride and the surrounding aqueous solution at the point of equilibrium and this P.D. is depressed in a similar way as the swelling of the gelatin chloride by the addition of neutral salts. It is shown that the P.D. can be calculated from the difference in the hydrogen ion concentration inside and outside the block of gelatin at equilibrium. 5. The influence of the hydrogen ion concentration on the P.D. of a gelatin chloride solution is similar to that of the hydrogen ion concentration on the osmotic pressure, swelling, and viscosity of gelatin solutions, and the same is true for the influence of the valency of the anion with which the gelatin is in combination. It is shown that in all these cases the P.D. which exists at equilibrium can be calculated with a fair degree of accuracy from the difference of the pH inside and outside the gelatin solution on the basis of Nernst's logarithmic formula by assuming that the difference in the concentration of hydrogen ions on both sides of the membrane determines the P.D. 6. The P.D. which exists at the boundary of a gelatin chloride solution and water at the point of equilibrium can also be calculated with a fair degree of accuracy by Nernst's logarithmic formula from the value pCl outside minus pCl inside. This proves that the equation x2 = y ( y + z) is the correct expression for the Donnan membrane equilibrium when solutions of protein-acid salts with monovalent anion are separated by a collodion membrane from water. In this equation x is the concentration of the H ion (and the monovalent anion) in the water, y the concentration of the H ion and the monovalent anion of the free acid in the gelatin solution, and z the concentration of the anion in combination with the protein. 7. The similarity between the variation of P.D. and the variation of the osmotic pressure, swelling, and viscosity of gelatin, and the fact that the Donnan equilibrium determines the variation in P.D. raise the question whether or not the variations of the osmotic pressure, swelling, and viscosity are also determined by the Donnan equilibrium.

scholarly journals HYDROPHILIC AND HYDROPHOBIC COLLOIDS AND THE INFLUENCE OF ELECTROLYTES ON MEMBRANE POTENTIALS AND CATAPHORETIC POTENTIALS

1924 ◽  
Vol 6 (3) ◽  
pp. 307-328 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Membrane Potentials ◽  
Ion Concentration ◽  
Protein Solutions ◽  
Depressing Effect ◽  
Hydrogen Ion Concentration ◽  
Donnan Equilibrium ◽  
Low Concentrations ◽  
Protein Gels ◽  
The Difference ◽  
Charging Effect

1. In order to be able to compare the effects of electrolytes on membrane potentials and cataphoretic potentials it seems necessary to distinguish between the charging and depressing effect of electrolytes on these potentials. Only low concentrations of acids and alkalies have a charging effect on the membrane potentials of proteins, while low concentrations of neutral salts have only a depressing effect; in the case of the cataphoretic potentials, low concentrations of salts have a charging effect as have also low concentrations of alkalies and in some cases low concentrations of acids. This difference finds its explanation in the difference of the origin of the two potentials and there can therefore be no common theory for the charging effect of electrolytes in the two cases. 2. There exists, however, an analogy in the depressing action of electrolytes on the two types of potentials inasmuch when the maximal P.D. is reached, all three kinds of electrolytes, acids, alkalies, and neutral salts, have a depressing effect on both types of potentials (taking into due consideration the effect of changes in the hydrogen ion concentration). 3. This depressing effect is adequately explained for the membrane potentials of protein solutions and protein gels on the basis of the Donnan equilibrium, and the question arises whether the same explanation may also hold for the cataphoretic potentials. 4. The active ion in the depressing action of electrolytes on membrane potentials as well as on cataphoretic potentials has the opposite sign of charge from that of the colloidal particle. It had been shown before that only the valency but not the chemical nature of the active ion determines the depressing effect in the case of membrane potentials and it is shown in this paper that the same is true for the cataphoretic potentials of particles of collodion, mastic, Acheson's graphite, and denatured egg albumin. 5. It is shown that the same valency rule holds also for the effect of acids on the cataphoretic potentials of collodion particles coated with gelatin, and that the ratio of the effect of dibasic to that of mono-basic acids is approximately 0.66, as Donnan's theory of membrane potentials would demand. 6. If we have a right to conclude from the validity of the valency rule for cataphoretic potentials that the depressing effect of electrolytes on the cataphoretic P.D. is determined by the Donnan equilibrium, we can understand the analogy between the depressing action of electrolytes on membrane potentials of hydrophilic colloids and on the cataphoretic potentials of hydrophobic colloids. We can also understand the analogy between the influence of electrolytes on the precipitation of hydrophobic colloids and on the depression of the values of all those properties of hydrophilic colloids which depend on the Donnan equilibrium, since the precipitation of hydrophobic colloids occurs when the cataphoretic P.D. is depressed below a critical value.

scholarly journals THE COLLOIDAL BEHAVIOR OF SERUM GLOBULIN

1922 ◽  
Vol 5 (1) ◽  
pp. 35-44 ◽  
Author(s):  
David I. Hitchcock
Keyword(s):  
Potential Difference ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Serum Globulin ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin ◽  
Electrometric Titration ◽  
Acids And Bases ◽  
Protein Serum ◽  
Colloidal Behavior

1. The globulin prepared from ox serum by dilution and precipitation with carbon dioxide has been found, by electrometric titration experiments, to behave like an amphoteric electrolyte, reacting stoichiometrically with acids and bases. 2. The potential difference developed between a solution of globulin chloride, phosphate, or acetate and a solution of the corresponding acid, free from protein, separated from the globulin by a collodion membrane, was found to be influenced by hydrogen ion concentration and salt concentration in the way predicted by Donnan's theory of membrane equilibrium. In experiments with sodium globulinate and sodium hydroxide it was found that the potential difference could be similarly explained. 3. The osmotic pressure of such solutions could be qualitatively accounted for by the Donnan theory, but exhibited a discrepancy which is explicable by analogy with certain experiments of Loeb on gelatin. 4. The application of Loeb's theory of colloidal behavior, which had previously been found to hold in the case of gelatin, casein, egg albumin, and edestin, has thus been extended to another protein, serum globulin.

scholarly journals ION SERIES AND THE PHYSICAL PROPERTIES OF PROTEINS

1921 ◽  
Vol 3 (3) ◽  
pp. 391-414 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Physical Properties ◽  
Osmotic Pressure ◽  
Opposite Sign ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Depressing Effect ◽  
Protein Solution ◽  
Hydrogen Ion Concentration ◽  
Specific Effects ◽  
Protein Ions

1. Ions with the opposite sign of charge as that of a protein ion diminish the swelling, osmotic pressure, and viscosity of the protein. Ions with the same sign of charge as the protein ion (with the exception of H and OH ions) seem to have no effect on these properties as long as the concentrations of electrolytes used are not too high. 2. The relative depressing effect of different ions on the physical properties of proteins is a function only of the valency and sign of charge of the ion, ions of the same sign of charge and the same valency having practically the same depressing effect on gelatin solutions of the same pH while the depressing effect increases rapidly with an increase in the valency of the ion. 3. The Hofmeister series of ions are the result of an error due to the failure to notice the influence of the addition of a salt upon the hydrogen ion concentration of the protein solution. As a consequence of this failure, effects caused by a variation in the hydrogen ion concentration of the solution were erroneously attributed to differences in the nature of the ions of the salts used. 4. It is not safe to draw conclusions concerning specific effects of ions on the swelling, osmotic pressure, or viscosity of gelatin when the concentration of electrolytes in the solution exceeds M/16, since at that concentration the values of these properties are near the minimum characteristic of the isoelectric point.

scholarly journals CHANGES IN THE APPARENT CYTOPLASMIC HYDROGEN ION CONCENTRATION OF AMEBA DUBIA ON INJECTION OF EGG ALBUMIN

1944 ◽  
Vol 28 (2) ◽  
pp. 95-102 ◽  
Author(s):  
A. Marshak
Keyword(s):  
Hydrogen Ion ◽  
Ion Concentration ◽  
Phenol Red ◽  
Alkaline Ph ◽  
Cent Solution ◽  
O2 Uptake ◽  
Marked Rise ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin ◽  
The One

1. Egg albumin when injected into an ameba or discharged into the solution about it raises the apparent pH of the cytoplasm of the ameba. 2. With time the cytoplasm returns to the original pH 6.9 if the nucleus is present. Amebae that have received repeated injections of albumin in some cases extrude their nuclei. In these cells the cytoplasm remains at the more alkaline pH induced by the albumin for at least 12 hours. 3. When a 2 per cent solution of albumin is introduced into a suspension of amebae there is a temporary marked rise in the rate at which CO2 is given off with no corresponding rise in O2 uptake. 4. The results observed can be explained if the albumin discharged onto the surface of the ameba rapidly enters the cell and there becomes distributed in a phase of the cytoplasm other than the one which contains the phenol red.

scholarly journals ELECTRICAL CHARGES OF COLLOIDAL PARTICLES AND ANOMALOUS OSMOSIS

1922 ◽  
Vol 4 (4) ◽  
pp. 463-486 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Isoelectric Point ◽  
Salt Solution ◽  
Electrical Transport ◽  
Colloidal Particles ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Trivalent Cation ◽  
Hydrogen Ion Concentration ◽  
Donnan Equilibrium ◽  
Positively Charged

1. It has been shown in previous publications that when solutions of different concentrations of salts are separated by collodion-gelatin membranes from water, electrical forces participate in addition to osmotic forces in the transport of water from the side of the water to that of the solution. When the hydrogen ion concentration of the salt solution and of the water on the other side of the membrane is the same and if both are on the acid side of the isoelectric point of gelatin (e.g. pH 3.0), the electrical transport of water increases with the valency of the cation and inversely with the valency of the anion of the salt in solution. Moreover, the electrical transport of water increases at first with increasing concentration of the solution until a maximum is reached at a concentration of about M/32, when upon further increase of the concentration of the salt solution the transport diminishes until a concentration of about M/4 is reached, when a second rise begins, which is exclusively or preeminently the expression of osmotic forces and therefore needs no further discussion. 2. It is shown that the increase in the height of the transport curves with increase in the valency of the cation and inversely with the increase in the valency of the anion is due to the influence of the salt on the P.D. (E) across the membrane, the positive charge of the solution increasing in the same way with the valency of the ions mentioned. This effect on the P.D. increases with increasing concentration of the solution and is partly, if not essentially, the result of diffusion potentials. 3. The drop in the transport curves is, however, due to the influence of the salts on the P.D. (ϵ) between the liquid inside the pores of the gelatin membrane and the gelatin walls of the pores. According to the Donnan equilibrium the liquid inside the pores must be negatively charged at pH 3.0 and this charge is diminished the higher the concentration of the salt. Since the electrical transport is in proportion to the product of E x ϵ and since the augmenting action of the salt on E begins at lower concentrations than the depressing action on ϵ, it follows that the electrical transport of water must at first rise with increasing concentration of the salt and then drop. 4. If the Donnan equilibrium is the sole cause for the P.D. (ϵ) between solid gelatin and watery solution the transport of water through collodion-gelatin membranes from water to salt solution should be determined purely by osmotic forces when water, gelatin, and salt solution have the hydrogen ion concentration of the isoelectric point of gelatin (pH = 4.7). It is shown that this is practically the case when solutions of LiCl, NaCl, KCl, MgCl2, CaCl2, BaCl2, Na2SO4, MgSO4 are separated by collodion-gelatin membranes from water; that, however, when the salt has a trivalent (or tetravalent?) cation or a tetravalent anion a P.D. between solid isoelectric gelatin and water is produced in which the wall assumes the sign of charge of the polyvalent ion. 5. It is suggested that the salts with trivalent cation, e.g. Ce(NO3)3, form loose compounds with isoelectric gelatin which dissociate electrolytically into positively charged complex gelatin-Ce ions and negatively charged NO3 ions, and that the salts of Na4Fe(CN)6 form loose compounds with isoelectric gelatin which dissociate electrolytically into negatively charged complex gelatin-Fe(CN)6 ions and positively charged Na ions. The Donnan equilibrium resulting from this ionization would in that case be the cause of the charge of the membrane.

scholarly journals ON THE INFLUENCE OF AGGREGATES ON THE MEMBRANE POTENTIALS AND THE OSMOTIC PRESSURE OF PROTEIN SOLUTIONS

1922 ◽  
Vol 4 (6) ◽  
pp. 769-776 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Membrane Potential ◽  
Hydrostatic Pressure ◽  
Osmotic Pressure ◽  
Membrane Potentials ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Gelatin Solution ◽  
True Solution ◽  
Hydrogen Ion Concentration ◽  
Donnan Equilibrium

1. It is shown that when part of the gelatin in a solution of gelatin chloride is replaced by particles of powdered gelatin (without change of pH) the membrane potential of the solution is influenced comparatively little. 2. A measurement of the hydrogen ion concentration of the gelatin chloride solution and the outside aqueous solution with which the gelatin solution is in osmotic equilibrium, shows that the membrane potential can be calculated from this difference of hydrogen ion concentration with an accuracy of half a millivolt. This proves that the membrane potential is due to the establishment of a membrane equilibrium and that the powdered particles participate in this membrane equilibrium. 3. It is shown that a Donnan equilibrium is established between powdered particles of gelatin chloride and not too strong a solution of gelatin chloride. This is due to the fact that the powdered gelatin particles may be considered as a solid solution of gelatin with a higher concentration than that of the weak gelatin solution in which they are suspended. It follows from the theory of membrane equilibria that this difference in concentration of protein ions must give rise to potential differences between the solid particles and the weaker gelatin solution. 4. The writer had shown previously that when the gelatin in a solution of gelatin chloride is replaced by powdered gelatin (without a change in pH), the osmotic pressure of the solution is lowered the more the more dissolved gelatin is replaced by powdered gelatin. It is therefore obvious that the powdered particles of gelatin do not participate in the osmotic pressure of the solution in spite of the fact that they participate in the establishment of the Donnan equilibrium and in the membrane potentials. 5. This paradoxical phenomenon finds its explanation in the fact that as a consequence of the participation of each particle in the Donnan equilibrium, a special osmotic pressure is set up in each individual particle of powdered gelatin which leads to a swelling of that particle, and this osmotic pressure is measured by the increase in the cohesion pressure of the powdered particles required to balance the osmotic pressure inside each particle. 6. In a mixture of protein in solution and powdered protein (or protein micellæ) we have therefore two kinds of osmotic pressure, the hydrostatic pressure of the protein which is in true solution, and the cohesion pressure of the aggregates. Since only the former is noticeable in the hydrostatic pressure which serves as a measure of the osmotic pressure of a solution, it is clear why the osmotic pressure of a protein solution must be diminished when part of the protein in true solution is replaced by aggregates.

A Comparison Between the Dissociation of the Haemocyanins of Helix and Crustacea

1926 ◽  
Vol 4 (2) ◽  
pp. 203-214
Author(s):  
LANCELOT T. HOGBEN ◽  
KATHLEEN F. PINHEY
Keyword(s):  
Helix Pomatia ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Dissociation Curve ◽  
Hydrogen Ion Concentration ◽  
Alkaline Side ◽  
Order Of Magnitude ◽  
N Gram ◽  
Increasing Temperature ◽  
Critical Ph

1. The effect of increasing temperature upon the dissociation curve of Helix is similar qualitatively to that which has been recorded in the case of haemoglobin and crustacean haemocyanin. The value of Q per n gram molecules of oxygen is about 8000 calories. That is, it is of the same order of magnitude as the value for crustacean haemocyanin, but in all probability significantly less. 2. The effect of increase of hydrogen-ion concentration upon the haemocyanin of Helix pomatia is remarkably slight as compared with its effect on crustacean haemocyanin. At low tensions no effect is detectable. Comparing the 50 per cent. and 75 per cent. saturation points, it is seen, that, as with crustacean haemocyanin, increasing hydrogen-ion concentration at first diminishes, but beyond a certain point increases, affinity for oxygen. The curves obtained on the acid side of this point are not identical in shape with the curves obtained on the alkaline side. The significance of this fact in relation to previous observations on crustacean haemocyanin, and to Rona and Ÿllpo's experiments on haemoglobin, is discussed in the text. 3. The behaviour of the haemocyanin of Helix as compared with that of crustacean haemocyanin in relation to the presence of neutral chlorides of the alkaline and alkaline earth metals is even more different. In alkaline medium, the addition of neutral chlorides to the serum depresses the dissociation curve; at a point on the acid side of the critical pH referred to in section 2, addition of salts was not found to exert any detectable influence.

scholarly journals THE EFFECT OF VARIOUS ACIDS ON THE DIGESTION OF PROTEINS BY PEPSIN

1919 ◽  
Vol 1 (6) ◽  
pp. 607-612 ◽  
Author(s):  
J. H. Northrop
Keyword(s):  
Acetic Acid ◽  
The State ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Pepsin Digestion ◽  
Marked Influence ◽  
Egg Albumin ◽  
Blood Albumin ◽  
Salt Action

1. At equal hydrogen ion concentration the rate of pepsin digestion of gelatin, egg albumin, blood albumin, casein, and edestin is the same in solutions of hydrochloric, nitric, sulfuric, oxalic, citric, and phosphoric acids. Acetic acid diminishes the rate of digestion of all the proteins except gelatin. 2. There is no evidence of antagonistic salt action in the effect of acids on the pepsin digestion of proteins. 3. The state of aggregation of the protein, i.e. whether in solution or not, and the viscosity of the solution have no marked influence on the rate of digestion of the protein.

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