scholarly journals THE ISOELECTRIC POINTS OF THE PROTEINS IN CERTAIN VEGETABLE JUICES

1919 ◽  
Vol 2 (2) ◽  
pp. 145-160 ◽  
Author(s):  
Edwin J. Cohn ◽  
Joseph Gross ◽  
Omer C. Johnson
Keyword(s):  
Electric Field ◽  
Isoelectric Point ◽  
The State ◽  
Hydrogen Ion ◽  
Tomato Juice ◽  
Ion Concentration ◽  
Carrot Juice ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Isoelectric Points

The state in which a protein substance exists depends upon the nature of its combination with acids or bases and is changed by change in the protein compound. The nature of the compound of a protein that exists at any hydrogen ion concentration can be ascertained if the isoelectric point of the protein is known. Accordingly information regarding the isoelectric points of vegetable proteins is of importance for operations in which it may be desirable to change the state of protein substances, as in the dehydration of vegetables. The Protein in Potato Juice.—The hydrogen ion concentration of the filtered juice of the potato is in the neighborhood of 10–7N. Such juice contains the globulin tuberin to the extent of from 1 to 2 per cent. The character of the compound of tuberin that exists in nature was suggested by its anodic migration in an electric field. The addition of acid to potato juice dissociated this compound and liberated tuberin at its isoelectric point. The isoelectric point of tuberin coincided with a slightly lower hydrogen ion concentration than 10–4N. At that reaction it existed most nearly uncombined. The flow of current during cataphoresis was greatest in the neighborhood of the isoelectric point. This evidence supplements that of the direction of the migration of tuberin, since it also suggests the existence of the greatest number of uncombined ions near this point. At acidities greater than the isoelectric point tuberin combined with acid. The compound that was formed contained nearly three times as much acid as was needed to dissociate the tuberin compound that existed in nature. At such acidities tuberin migrated to the cathode. Though never completely precipitated tuberin was least soluble in the juice of the potato in the neighborhood of its isoelectric point. Both the compounds of tuberin with acids and with bases were more soluble in the juice than was uncombined tuberin. The nature of the slight precipitate that separated when potato juice was made slightly alkaline was not determined. The Protein in Carrot Juice.—The isoelectric point of the protein in carrot juice coincided with that of tuberin. Remarkably similar also were the properties of carrot juice and the juice of the potato. Existing in nature at nearly the same reaction they combined with acids and bases to nearly the same extent and showed minima in solubility at the same hydrogen ion concentrations. The greatest difference in behavior concerned the alkaline precipitate which, in the carrot, was nearly as great as the acid precipitate. The Protein in Tomato Juice.—The protein of the tomato existed in a precipitated form near its isoelectric point. Accordingly it was not present to any extent in filtered tomato juice. If, however, the considerable acidity at which the tomato exists was neutralized the protein dissolved and was filterable. It then migrated to the anode in an electric field. The addition of sufficient acid to make the hydrogen ion concentration slightly greater than 10–5N again precipitated the protein at its isoelectric point. At greater acidities migration was cathodic.

scholarly journals THE RELATION OF THE PNEUMOCOCCUS TO HYDROGEN ION CONCENTRATION, ACID DEATH-POINT, AND DISSOLUTION OF THE ORGANISM

1919 ◽  
Vol 30 (4) ◽  
pp. 389-399 ◽  
Author(s):  
Frederick T. Lord ◽  
Robert N. Nye
Keyword(s):  
Hydrogen Ion ◽  
Ion Concentration ◽  
Direct Relation ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Cent Glucose ◽  
Fluid Media

1. In the growth and death of the pneumococcus in fluid media containing 1 per cent glucose the production of acid is the most important bactericidal factor. 2. 1 per cent glucose bouillon cultures of the pneumococcus allowed to grow and die out usually reach a final acidity of a pH of about 5.1. 3. At a hydrogen ion concentration of about 5.1 or higher, the pneumococcus does not survive longer than a few hours. 4. In hydrogen ion concentrations of about 6.8 to 7.4 the pneumococcus may live for at least many days. 5. In the intervening hydrogen ion concentrations, between 6.8 and 5.1, the pneumococcus is usually killed with a rapidity which bears a direct relation to the hydrogen ion concentration; i.e., the greater the acidity the more rapid is the death. 6. Cloudy suspensions of washed pneumococci in hydrogen ion concentrations varying from 8.0 to 4.0 show, after incubation, dissolution of organisms in lower hydrogen ion concentrations than about 5.0. This dissolution is most marked at about 5.0 to 6.0. Some dissolution also takes place toward the more alkaline end of the scale. No dissolution occurs at the most acid end of the scale.

scholarly journals THE RELATION OF PROTEOLYTIC ENZYMES IN THE PNEUMONIC LUNG TO HYDROGEN ION CONCENTRATION. AN EXPLANATION OF RESOLUTION

1919 ◽  
Vol 30 (4) ◽  
pp. 379-388 ◽  
Author(s):  
Frederick T. Lord
Keyword(s):  
Amino Acid ◽  
Proteolytic Enzyme ◽  
Gradual Increase ◽  
Cellular Material ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Acid Media ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Amino Acid Nitrogen

Evidence is given of the presence in the cellular material obtained from the pneumonic lung of a proteolytic enzyme digesting coagulated blood serum at hydrogen ion concentrations of 7.3 to 6.7 and inactive at higher; i.e., more acid concentrations. In addition, evidence is brought forward of the presence in the cellular material from the pneumonic lung of a proteolytic enzyme splitting peptone to amino-acid nitrogen. This enzyme is operative at hydrogen ion concentrations from 8.0 to 4.8, but most active at 6.3 or 5.2. These findings may be regarded as having a bearing on resolution in pneumonia. During the course of the disease a gradual increase in the hydrogen ion concentration of the exudate probably takes place. With the breaking down of cellular material an enzyme digesting protein (fibrin) in weakly alkaline and weakly acid media may be liberated. With a gradual increase in the hydrogen ion concentration of the pneumonic lung the action of this enzyme probably ceases. An enzyme capable of splitting peptone to amino-acid nitrogen is probably active during the proteolysis of the fibrin and further activated when the hydrogen ion concentration of the pneumonic lung is increased to within its range of optimum activity at a pH of 6.3 and 5.2. By this means it may be conceived that the exudate is dissolved and resolution takes place.

scholarly journals THE OPTIMUM HYDROGEN ION CONCENTRATION FOR THE GROWTH OF PNEUMOCOCCUS

1918 ◽  
Vol 28 (3) ◽  
pp. 345-357 ◽  
Author(s):  
K. G. Dernby ◽  
O. T. Avery
Keyword(s):  
Salt Concentration ◽  
Culture Media ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Initial Reaction ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations

1. The optimum hydrogen ion concentration for the growth of the various types of pneumococcus is a pH of about 7.8. 2. The limiting hydrogen ion concentrations for the growth of pneumococcus are a pH of 7.0 and a pH of 8.3. 3. Phosphates used in adjusting reactions of media retard growth if present in a concentration greater than 0.1 molecular. 4. Culture media for pneumococci should, therefore, have an initial reaction between a pH of 7.8 and 8.0 and a total salt concentration not exceeding 0.1 M.

scholarly journals AMPHOTERIC COLLOIDS

1918 ◽  
Vol 1 (2) ◽  
pp. 237-254 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Isoelectric Point ◽  
Water Solubility ◽  
Biological Significance ◽  
Volumetric Analysis ◽  
The Body ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Sharp Drop ◽  
Hydrogen Ion Concentration ◽  
Alkaline Side

1. It is shown by volumetric analysis that on the alkaline side from its isoelectric point gelatin combines with cations only, but not with anions; that on the more acid side from its isoelectric point it combines only with anions but not with cations; and that at the isoelectric point, pH = 4.7, it combines with neither anion nor cation. This confirms our statement made in a previous paper that gelatin can exist only as an anion on the alkaline side from its isoelectric point and only as a cation on the more acid side of its isoelectric point, and practically as neither anion nor cation at the isoelectric point. 2. Since at the isoelectric point gelatin (and probably amphoteric colloids generally) must give off any ion with which it was combined, the simplest method of obtaining amphoteric colloids approximately free from ionogenic impurities would seem to consist in bringing them to the hydrogen ion concentration characteristic of their isoelectric point (i.e., at which they migrate neither to the cathode nor anode of an electric field). 3. It is shown by volumetric analysis that when gelatin is in combination with a monovalent ion (Ag, Br, CNS), the curve representing the amount of ion-gelatin formed is approximately parallel to the curve for swelling, osmotic pressure, and viscosity. This fact proves that the influence of ions upon these properties is determined by the chemical or stoichiometrical and not by the "colloidal" condition of gelatin. 4. The sharp drop of these curves at the isoelectric point finds its explanation in an equal drop of the water solubility of pure gelatin, which is proved by the formation of a precipitate. It is not yet possible to state whether this drop of the solubility is merely due to lack of ionization of the gelatin or also to the formation of an insoluble tautomeric or polymeric compound of gelatin at the isoelectric point. 5. On account of this sudden drop slight changes in the hydrogen ion concentration have a considerably greater chemical and physical effect in the region of the isoelectric point than at some distance from this point. This fact may be of biological significance since a number of amphoteric colloids in the body seem to have their isoelectric point inside the range of the normal variation of the hydrogen ion concentration of blood, lymph, or cell sap. 6. Our experiments show that while a slight change in the hydrogen ion concentration increases the water solubility of gelatin near the isoelectric point, no increase in the solubility can be produced by treating gelatin at the isoelectric point with any other kind of monovalent or polyvalent ion; a fact apparently not in harmony with the adsorption theory of colloids, but in harmony with a chemical conception of proteins.

scholarly journals The influence of hydrogen-ion concentration upon the adsorption of weak electrolytes by pure charcoal.—Part II

1931 ◽  
Vol 133 (821) ◽  
pp. 155-161 ◽  
Keyword(s):  
The Other ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Adsorption From Solutions ◽  
Ion Concentrations ◽  
Preferential Adsorption ◽  
Chemical Combination ◽  
Weak Electrolytes ◽  
Adsorption Curve

In a recent communication results were described which indicate that propionic, hexoic, and succinic acids are adsorbed by purified charcoal only as unionised molecules. There was no evidence that anions of these acids were adsorbed to any measurable extent. Thus the amount of these acids adsorbed from mixed solutions of any one acid and its sodium salt is propor­tional to the amount of unionised acid present as calculated from the known ionisation constants and the hydrogen-ion concentration of the solutions. Further work has led to the conclusion that the presence of an unionised carboxyl group is essential for adsorption to take place. On the other hand, the adsorption curve for the bases n -propylamine and n -butylamine at different hydrogen-ion concentrations did not follow the ionisation curves very closely.Strong preferential adsorption of the unionised molecule was observed but there was quite considerable adsorption from solutions of such acidity that no unionised amine could exist in them. The adsorption of both bases was found to fall off gradually and continuously with increasing acidity from p H 11 to P H 3. In view of the fact that the charcoal used in this work was Norit charcoal purified by treatment with strong halogen acids, it was thought possible that very small traces of these acids remained after the washing to which the char­coal was subjected, and that these traces of acid caused the adsorption of basic ions by direct chemical combination.

scholarly journals THE ELIMINATION OF DISCREPANCIES BETWEEN OBSERVED AND CALCULATED P.D. OF PROTEIN SOLUTIONS NEAR THE ISOELECTRIC POINT WITH THE AID OF BUFFER SOLUTIONS

1922 ◽  
Vol 4 (5) ◽  
pp. 617-619 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Aqueous Solution ◽  
Aqueous Solutions ◽  
Isoelectric Point ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Protein Solutions ◽  
Protein Solution ◽  
Hydrogen Ion Concentration ◽  
Buffer Salt ◽  
Buffer Solutions

1. It had been noticed in the previous experiments on the influence of the hydrogen ion concentration on the P.D. between protein solutions inside a collodion bag and aqueous solutions free from protein that the agreement between the observed values and the values calculated on the basis of Donnan's theory was not satisfactory near the isoelectric point of the protein solution. It was suspected that this was due to the uncertainty in the measurements of the pH of the outside aqueous solution near the isoelectric point. This turned out to be correct, since it is shown in this paper that the discrepancy disappears when both the inside and outside solutions contain a buffer salt. 2. This removes the last discrepancy between the observed P.D. and the P. D. calculated on the basis of Donnan's theory of P.D. between membrane equilibria, so that we can state that the P.D. between protein solutions inside collodion bags and outside aqueous solutions free from protein can be calculated from differences in the hydrogen ion concentration on the opposite sides of the membrane, in agreement with Donnan's formula.

THE EFFECT OF TEMPERATURE AND pH ON THE LONGEVITY OF SCHISTOSOMATIUM DOUTHITTI MIRACIDIA

1962 ◽  
Vol 40 (4) ◽  
pp. 615-620 ◽  
Author(s):  
J. Farley
Keyword(s):  
Half Life ◽  
Large Population ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Effect Of Temperature ◽  
Critical Factors ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Constant Ph

Observations made on the effect of various temperatures and hydrogen ion concentrations on the longevity of Schistosomatium douthitti miracidia showed both to be critical factors. The half-life of the miracidia varied from 1.5 hours at 35 °C to 11 hours at 8 °C, at a constant pH of 7.3. The effect of hydrogen ion concentration was less pronounced, the optimum being pH 7.5. A large population of miracidia from a single liver continued hatching over a 4-hour period with a peak output occurring at half an hour and another at 1 hour after exposure to water. The longevity of the miracidia hatching within the first hour exceeded that of the larvae hatching later.

scholarly journals THE MECHANISM OF COMPLEMENT ACTION

1920 ◽  
Vol 3 (2) ◽  
pp. 185-201
Author(s):  
S. C. Brooks
Keyword(s):  
Surface Tension ◽  
Serum Proteins ◽  
Ultra Violet ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Ultra Violet Light ◽  
Violet Light ◽  
Molecular Group

It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of complement is not a result of any changes in hydrogen ion concentration since these are less than 0.05 pH. 4. That hydrogen ion concentrations high enough to transform serum proteins from the cation to the anion condition (i.e. past the isoelectric point) permanently inactivate complement. These facts together with those given in previous papers lead to the following hypotheses. 1. That there is present in serum a hemolytic substance which is formed from a precursor (which may resemble lecithin) and is constantly being formed and simultaneously being broken down into inactive products. 2. That both precursor and lysin contain the same photosensitive molecular group. 3. That the lytic substance is dependent for its activity upon the state of the serum proteins.

The Influence of Hydrogen-ion Concentration on Some Acid Resistant Bacteria

1938 ◽  
Vol 4a (3) ◽  
pp. 219-227
Author(s):  
Dennis W. Watson
Keyword(s):  
Living Cell ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Resistant Bacteria ◽  
Limited Growth ◽  
Genus Bacillus ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Bacillus Strains

Fifty-three strains of bacteria have been isolated from acidulated brine. They are classified into Bacillus, Micrococcus, Sarcina, and Lactobacillus. Of these the Bacillus strains failed to grow at hydrogen-ion concentrations more acid than pH 6.20, while the Micrococcus and Sarcina forms showed a greater tolerance, producing limited growth from pH 5.22 to 5.64. Other workers describing wider limits for the genus Bacillus failed to allow for the change produced in the weakly buffered environment by the living cell. The microaerophilic Lactobacilli grew at pH 3.52. These aciduric types are not actively proteolytic.

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.

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