scholarly journals The osmotic pressure of crystalline egg-albumin

1929 ◽  
Vol 23 (5) ◽  
pp. 1079-1089 ◽  
Author(s):  
John Marrack ◽  
Leslie Frank Hewitt
Keyword(s):  
Osmotic Pressure ◽  
Egg Albumin

scholarly journals THE KINETICS OF OSMOSIS

1927 ◽  
Vol 10 (6) ◽  
pp. 883-892 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
Osmotic Pressure ◽  
Egg Albumin ◽  
Kinetics Of

It is shown that by combining the osmotic pressure and rate of diffusion laws an equation can be derived for the kinetics of osmosis. The equation has been found to agree with experiments on the rate of osmosis for egg albumin and gelatin solutions with collodion membranes.

scholarly journals ION SERIES AND THE PHYSICAL PROPERTIES OF PROTEINS. I

1920 ◽  
Vol 3 (1) ◽  
pp. 85-106 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Oxalic Acid ◽  
Physical Properties ◽  
Osmotic Pressure ◽  
Chloride Solution ◽  
Dibasic Acid ◽  
Egg Albumin ◽  
Phosphoric Acids ◽  
Acid Salts

1. This paper contains experiments on the influence of acids and alkalies on the osmotic pressure of solutions of crystalline egg albumin and of gelatin, and on the viscosity of solutions of gelatin. 2. It was found in all cases that there is no difference in the effects of HCl, HBr, HNO3, acetic, mono-, di-, and trichloracetic, succinic, tartaric, citric, and phosphoric acids upon these physical properties when the solutions of the protein with these different acids have the same pH and the same concentration of originally isoelectric protein. 3. It was possible to show that in all the protein-acid salts named the anion in combination with the protein is monovalent. 4. The strong dibasic acid H2SO4 forms protein-acid salts with a divalent anion SO4 and the solutions of protein sulfate have an osmotic pressure and a viscosity of only half or less than that of a protein chloride solution of the same pH and the same concentration of originally isoelectric protein. Oxalic acid behaves essentially like a weak dibasic acid though it seems that a small part of the acid combines with the protein in the form of divalent anions. 5. It was found that the osmotic pressure and viscosity of solutions of Li, Na, K, and NH4 salts of a protein are the same at the same pH and the same concentration of originally isoelectric protein. 6. Ca(OH)2 and Ba(OH)2 form salts with proteins in which the cation is divalent and the osmotic pressure and viscosity of solutions of these two metal proteinates are only one-half or less than half of that of Na proteinate of the same pH and the same concentration of originally isoelectric gelatin. 7. These results exclude the possibility of expressing the effect of different acids and alkalies on the osmotic pressure of solutions of gelatin and egg albumin and on the viscosity of solutions of gelatin in the form of ion series. The different results of former workers were probably chiefly due to the fact that the effects of acids and alkalies on these proteins were compared for the same quantity of acid and alkali instead of for the same pH.

scholarly journals ELECTROKINETIC PHENOMENA

1932 ◽  
Vol 15 (5) ◽  
pp. 605-610
Author(s):  
Harold A. Abramson ◽  
E. B. Grossman
Keyword(s):  
Osmotic Pressure ◽  
Titration Curve ◽  
Specific Rotation ◽  
Protein Solutions ◽  
Net Charge ◽  
Electrokinetic Phenomena ◽  
Egg Albumin

The specific rotation of egg albumin, gliadin, and gelatin (40°C.) is discussed in connection with available data on (a) mobility, (b) titration curve, and (c) osmotic pressure. It seems likely that the change in specific rotation with pH of protein solutions is proportional to the change in net charge.

scholarly journals OSMOTIC PRESSURE OF EGG ALBUMIN SOLUTIONS

1941 ◽  
Vol 137 (1) ◽  
pp. 143-151
Author(s):  
Henry B. Bull
Keyword(s):  
Osmotic Pressure ◽  
Egg Albumin

scholarly journals DONNAN EQUILIBRIUM AND THE PHYSICAL PROPERTIES OF PROTEINS

1921 ◽  
Vol 3 (5) ◽  
pp. 691-714 ◽  
Author(s):  
Jacques Loeb
Keyword(s):  
Osmotic Pressure ◽  
Free Acid ◽  
Ph Effect ◽  
Ion Concentration ◽  
Relative Distribution ◽  
Acid Salt ◽  
Unequal Distribution ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin ◽  
Fair Degree

1. It had been shown in previous publications that the osmotic pressure of a 1 per cent solution of a protein-acid salt varies in a characteristic way with the hydrogen ion concentration of the solution, the osmotic pressure having a minimum at the isoelectric point, rising steeply with a decrease in pH until a maximum is reached at pH of 3.4 or 3.5 (in the case of gelatin and crystalline egg albumin), this maximum being followed by a steep drop in the osmotic pressure with a further decrease in the pH of the gelatin or albumin solution. In this paper it is shown that (aside from two minor discrepancies) we can calculate this effect of the pH on the osmotic pressure of a protein-acid salt by assuming that the pH effect is due to that unequal distribution of crystalloidal ions (in particular free acid) on both sides of the membrane which Donnan's theory of membrane equilibrium demands. 2. It had been shown in preceding papers that only the valency but not the nature of the ion (aside from its valency) with which a protein is in combination has any effect upon the osmotic pressure of the solution of the protein; and that the osmotic pressure of a gelatin-acid salt with a monovalent anion (e.g. Cl, NO3, acetate, H2PO4, HC2O4, etc.) is about twice or perhaps a trifle more than twice as high as the osmotic pressure of gelatin sulfate where the anion is bivalent; assuming that the pH and gelatin concentrations of all the solutions are the same. It is shown in this paper that we can calculate with a fair degree of accuracy this valency effect on the assumption that it is due to the influence of the valency of the anion of a gelatin-acid salt on that relative distribution of the free acid on both sides of the membrane which Donnan's theory of membrane equilibrium demands. 3. The curves of the observed values of the osmotic pressure show two constant minor deviations from the curves of the calculated osmotic pressure. One of these deviations consists in the fact that the values of the ascending branch of the calculated curves are lower than the corresponding values in the curves for the observed osmotic pressure, and the other deviation consists in the fact that the drop in the curves of calculated values occurs at a lower pH than the drop in the curves of the observed values.

scholarly journals STUDIES ON THE REGULATION OF OSMOTIC PRESSURE

1922 ◽  
Vol 4 (5) ◽  
pp. 585-589 ◽  
Author(s):  
Walter W. Palmer ◽  
Dana W. Atchley ◽  
Robert F. Loeb
Keyword(s):  
Osmotic Pressure ◽  
Isoelectric Point ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Nacl Solution ◽  
Hydrogen Ion Concentration ◽  
Egg Albumin

Egg albumin, like gelatin, influences the conductivity of a 0.6 per cent NaCl solution in two ways: (a) At an hydrogen ion concentration of about pH 3.0, increasing concentrations increase the conductivity. (b) Near the isoelectric point of albumin and at the pH of the blood, increasing concentrations of albumin decrease the conductivity of the NaCl solution.

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