scholarly journals THE COLLOIDAL BEHAVIOR OF EDESTIN

1922 ◽  
Vol 4 (5) ◽  
pp. 597-615 ◽  
Author(s):  
David I. Hitchcock

1. It has been shown by titration experiments that the globulin edestin behaves like an amphoteric electrolyte, reacting stoichiometrically with acids and bases. 2. The potential difference developed between a solution of edestin chloride or acetate separated by a collodion membrane from an acid solution free from protein was found to be influenced by salt concentration and hydrogen ion concentration in the way predicted by Donnan's theory of membrane equilibrium. 3. The osmotic pressure of such edestin-acid salt solutions was found to be influenced by salt concentration and by hydrogen ion concentration in the same way as is the potential difference. 4. The colloidal behavior of edestin is thus completely analogous to that observed by Loeb with gelatin, casein, and egg albumin, and may be explained by Loeb's theory of colloidal behavior, which is based on the idea that proteins react stoichiometrically as amphoteric electrolytes and on Donnan's theory of membrane equilibrium.

1922 ◽  
Vol 5 (1) ◽  
pp. 35-44 ◽  
Author(s):  
David I. Hitchcock

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.


1927 ◽  
Vol 8 (6) ◽  
pp. 543-599 ◽  
Author(s):  
S. P. L. Sørensen ◽  
K. Linderstrøm-Lang ◽  
Ellen Lund

Introduction. A description is given of the principle followed in the experimental determination of the ionisation of egg albumin, its capacity to combine with acids and bases. Egg albumin is regarded as an ampholyte, and in accordance with J. N. Brønsted's definition of acids and bases, ampholytes are considered as substances capable of both taking up and giving off hydrogen ions. The theoretical treatment of the capacity of ampholytes to combine with acids (and bases) has been carried out on this basis. Section A. Several experimental series are noted, comprising the determination of the activity coefficient of the hydrogen ion (fH) in ammonium chloride solutions of different concentration. Section B. The general method of experimental determination of the ionisation (capacity to combine with adds and bases) of egg albumin in ammonium chloride and potassium chloride solutions is briefly described, and the results of the experiments are compared. Section C. 1). In a brief theoretical survey we have suggested that distinction should be made between isoelectric and isoionic reaction of an ampholyte, the former defined as the hydrogen ion activity (value of paH) at which the mean valency of the ampholyte is 0, the latter as the hydrogen ion activity at which the quantity of acid or base combined with the ampholyte is 0; or, as we prefer to express it, the hydrogen ion activity at which the specific hydrogen ionisation of the ampholyte is 0. If the ampholyte does not combine with other ions than the hydrogen ion, then isoelectric and isoionic reaction coincide. Isoionic reaction is determined by acid-combining experiments. The principle of this determination is briefly described. A theoretical investigation of the alteration with salt concentration of both isoelectric (isoionic) reaction and the shape and direction of the ionisation curves is made, with regard to ampholytes capable only of combining with hydrogen ions, on the basis of the Debye-Hückel formulæ and Linderstrøm-Lang's theory for the ionisation of polyvalent ampholytes of simple type. It is shown that the salt effect, in accordance with the theory, and in qualitative agreement with the experiments, consists in a turning of the ionisation curves, indicating the relation between the quantity of combined acid (specific hydrogen ionisation) and paH, and the turning of the curves, which leaves the isoelectric reaction unaltered, tends in such a direction that the quantity of combined acid at constant ampholyte concentration and constant pan increases with increasing salt concentration. The possibility of chemical combining of other ions than the hydrogen ion is discussed. 2). Following on 1), a brief survey of the experimental results is given. 3). The isoionic reaction is found from the experimental material and proved to be independent of the ammonium chloride concentration. As the mean of all determinations we have paH0 = 4.898 (isoionic reaction). The difference between this value and that formerly found for ammonium sulphate solutions (4.844) is discussed. 4). Finally, on the basis of the theory in Section 1), some simple calculations of the ionisation curves for egg albumin are made, and it appears that the theory can reproduce the experimental results in a rough quantitative way when we assume that the egg albumin has a radius of 2.21·10–7 cm. (answering to a molecular weight of 35,000 in aqueous solution), and contains 30 acid and base groups.


1918 ◽  
Vol 28 (3) ◽  
pp. 345-357 ◽  
Author(s):  
K. G. Dernby ◽  
O. T. Avery

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.


1944 ◽  
Vol 28 (2) ◽  
pp. 95-102 ◽  
Author(s):  
A. Marshak

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.


1919 ◽  
Vol 1 (6) ◽  
pp. 607-612 ◽  
Author(s):  
J. H. Northrop

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.


1920 ◽  
Vol 2 (5) ◽  
pp. 577-594 ◽  
Author(s):  
Jacques Loeb

1. It had been shown in previous papers that when a collodion membrane has been treated with a protein the membrane assumes a positive charge when the hydrogen ion concentration of the solution with which it is in contact exceeds a certain limit. It is pointed out in this paper that by treating the collodion membrane with a protein (e.g. oxyhemoglobin) a thin film of protein adheres to the membrane and that the positive charge of the membrane must therefore be localized in this protein film. 2. It is further shown in this paper that the hydrogen ion concentration, at which the reversal in the sign of the charge of a collodion membrane treated with a protein occurs, varies in the same sense as the isoelectric point of the protein, with which the membrane has been treated, and is always slightly higher than that of the isoelectric point of the protein used. 3. The critical hydrogen ion concentration required for the reversal seems to be, therefore, that concentration where enough of the protein lining of the membrane is converted into a protein-acid salt (e.g. gelatin nitrate) capable of ionizing into a positive protein ion (e.g. gelatin) and the anion of the acid used (e.g. NO3).


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