THE INFLUENCE OF MEMBRANE PREPARATION ON THE OSMOTIC PRESSURE OF POLYVINYL ACETATE IN ACETONE

1946 ◽  
Vol 24b (4) ◽  
pp. 150-166 ◽  
Author(s):  
R. E. Robertson ◽  
R. McIntosh ◽  
W. E. Grummitt
Keyword(s):  
Sodium Hydroxide ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Polyvinyl Acetate ◽  
Membrane Surface ◽  
Membrane Preparation ◽  
Adequate Explanation ◽  
Full Account ◽  
Molecular Weights ◽  
Large Ratio

A full account of the experimental procedures used to determine the number average molecular weights of a series of polyvinyl acetates is given. Adsorption of polyvinyl acetate on a cellophane membrane is demonstrated. The importance of this phenomenon is increased when cells of large ratio of membrane surface to cell volume are used. The presence of small amounts of sodium hydroxide in the membrane eliminates detectable adsorption and alters the osmotic pressure values. This change does not appear to be due to imperfect semipermeability of the membranes, and no adequate explanation of the phenomenon has been as yet discovered.

Colloid osmotic pressure changes of dog's blood exposed to different mixtures of CO2 and air

1978 ◽  
Vol 44 (2) ◽  
pp. 254-257 ◽  
Author(s):  
Y. Kakiuchi ◽  
A. B. DuBois ◽  
D. Gorenberg
Keyword(s):  
Red Blood Cells ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Blood Cells ◽  
Freezing Point ◽  
Colloid Osmotic Pressure ◽  
Red Cell ◽  
Freezing Point Depression ◽  
Pressure Changes ◽  
Different Levels

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.

scholarly journals OSMOTIC PRESSURE STUDY OF PROTEIN FRACTIONS IN NORMAL AND IN NEPHROTIC SUBJECTS

1939 ◽  
Vol 69 (6) ◽  
pp. 819-831 ◽  
Author(s):  
Jaques Bourdillon
Keyword(s):  
Osmotic Pressure ◽  
Normal Serum ◽  
The Other ◽  
Protein Fractions ◽  
Molecular Weights ◽  
Other Hand ◽  
Normal Albumin

In serum of patients with nephrosis both albumin and globulin showed by osmotic pressure nearly double the molecular weights of normal albumin and globulin. In the urines of such patients, on the other hand, both proteins showed molecular weights lower even than in normal serum. The colloidal osmotic pressures were measured by the author's method at such dilutions that the van't Hoff law relating pressures to molecular concentrations could be directly applied. For the albumin and globulin of normal serum the molecular weights found were 72,000 and 164,000 respectively, in agreement with the weights obtained by other methods.

Effect of basement membrane and colloid osmotic pressure on renal tubule cell volume

1977 ◽  
Vol 233 (4) ◽  
pp. F325-F332
Author(s):  
M. A. Linshaw ◽  
F. B. Stapleton ◽  
F. E. Cuppage ◽  
J. J. Grantham
Keyword(s):  
Basement Membrane ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Cell Size ◽  
Renal Tubule ◽  
Colloid Osmotic Pressure ◽  
Outer Diameter ◽  
Tubule Cell ◽  
Cation Pump ◽  
Renal Tubule Cell

Renal tubule cell volume is thought to be kept constant by a cation pump. When active transport is blocked, intracellular impermeant solutes cause cells to swell. Cell size is then determined by transmembrane hydrostatic and colloid osmotic forces. We studied the importance of passive transmembrane forces in determining cell size in isolated rabbit proximal straight tubules (PST). We blocked active solute transport with ouabain and evaluated subsequent changes in cell size by measuring outer diameter of nonperfused tubules. Tubules in a ouabain and 6 g/100 ml protein bath swelled only 40% above control. However, removal of the tubule basement membrane with collagenase dissipated a transmembrane hydrostatic pressure and caused more swelling. Final cell volume was determined largely by bath protein concentration. Tubules in ouabain and collagenase swelled enormously in hyponcotic protein, moderately in isoncotic protein, and could be shrunk below control in hyperoncotic protein. Intracellular colloid osmotic pressure was estimated to exceed 38 cmH20. We conclude that hydrostatic and colloid osmotic forces are major determinants of cell size in isolated PST treated with ouabain.

Correlation between osmoregulation and cell volume regulation

1987 ◽  
Vol 252 (4) ◽  
pp. R768-R773
Author(s):  
M. A. Lang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Free Amino Acids ◽  
Volume Regulation ◽  
Free Amino ◽  
Cell Volume Regulation

The euryhaline crab, Callinectes sapidus, behaves both as an osmoregulator when equilibrated in salines in the range of 800 mosM and below and an osmoconformer when equilibrated in salines above 800 mosM. There exists a close correlation between osmoregulation seen in the whole animal in vivo and cell volume regulation studied in vitro. Hyperregulation of the hemolymph osmotic pressure and cell volume regulation both occurred in salines at approximately 800 mosM and below. During long-term equilibration of the crabs to a wide range of saline environments, the total concentration of hemolymph amino acids plus taurine remained below 3 mM. During the first 6 h after an acute osmotic stress to the whole animal, the hemolymph osmotic pressure and Na activity gradually decreased, whereas the free amino acids remained below 3 mM. As the hemolymph osmotic pressure decreased below approximately 850 mosM, the amino acid level began to increase to 17-25 mM. This change was primarily due to increases in glycine, proline, taurine, and alanine. The likely source of the increase in hemolymph free amino acids in vivo is the free amino acid loss from muscle cells observed during cell volume regulation in vitro.

scholarly journals Concurrent changes in Dunaliella salina ultrastructure and membrane phospholipid metabolism after hyperosmotic shock.

1988 ◽  
Vol 107 (2) ◽  
pp. 529-538 ◽  
Author(s):  
K J Einspahr ◽  
M Maeda ◽  
G A Thompson
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Volume ◽  
Surface Area ◽  
Dunaliella Salina ◽  
Membrane Surface ◽  
Fold Increase ◽  
Phospholipid Metabolism ◽  
Hyperosmotic Shock ◽  
Nacl Concentration ◽  
Intracellular Organelles

Hyperosmotic shock, induced by raising the NaCl concentration of Dunaliella salina medium from 1.71 to 3.42 M, elicited a rapid decrease of nearly one-third in whole cell volume and in the volume of intracellular organelles. The decrease in cell volume was accompanied by plasmalemma infolding without overall loss of surface area. This contrasts with the dramatic increase in plasmalemma surface area after hypoosmotic shock (Maeda, M., and G. A. Thompson. 1986. J. Cell Biol. 102:289-297). Although plasmalemma surface area remained constant after hyperosmotic shock, the nucleus, chloroplast, and mitochondria lost membrane surface area, apparently through membrane fusion with the endoplasmic reticulum. Thus the endoplasmic reticulum serves as a reservoir for excess membrane during hyperosmotic stress, reversing its role as membrane donor to the same organelles during hypoosmotically induced cell expansion. Hyperosmotic shock also induced rapid changes in phospholipid metabolism. The mass of phosphatidic acid dropped to 56% of control and that of phosphatidylinositol 4,5-bisphosphate rose to 130% of control within 4 min. Further analysis demonstrated that within 10 min after hyperosmotic shock, there was 2.5-fold increase in phosphatidylcholine turnover, a twofold increase in lysophosphatidylcholine mass, a four-fold increase in lysophosphatidate mass, and an elevation in free fatty acids to 124% of control, all observations suggesting activation of phospholipase A. The observed biophysical and biochemical phenomena are likely to be causally interrelated in providing mechanisms for successful accommodation to such severe osmotic extremes.

Membranes for measuring Low Molecular Weights by Osmotic Pressure

Nature ◽  
1967 ◽  
Vol 213 (5077) ◽  
pp. 692-693 ◽  
Author(s):  
J. R. H. WAKE ◽  
A. M. POSNER
Keyword(s):  
Osmotic Pressure ◽  
Molecular Weights

THE MOLECULAR WEIGHT OF POLYVINYL ACETATE

1958 ◽  
Vol 36 (3) ◽  
pp. 543-549 ◽  
Author(s):  
A. F. Sirianni ◽  
R. Tremblay ◽  
I. E. Puddington
Keyword(s):  
Molecular Weight ◽  
Vapor Pressure ◽  
Polyvinyl Acetate ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Molecular Weights ◽  
Approximate Molecular Weight ◽  
Low Degrees ◽  
Made In

The molecular weights of a series of unfractionated polyvinyl acetates of low degrees of polymerization have been measured by determining the lowering of the vapor pressure of their solutions. An approximate molecular-weight range of 5000–40,000 was examined. While most of the determinations were made in benzene solutions at 55 °C., other solvents and temperatures were used. Anomalous results were obtained with one sample of fractionated material.

THE NUMBER OF SUBUNITS IN THE MOLECULE OF HORSE HEMOGLOBIN

1956 ◽  
Vol 34 (4) ◽  
pp. 411-425 ◽  
Author(s):  
M. E. Reichmann ◽  
J. Ross Colvin
Keyword(s):  
Light Scattering ◽  
Osmotic Pressure ◽  
Performic Acid ◽  
Approach To Equilibrium ◽  
Salt Solutions ◽  
Covalent Bonds ◽  
Molecular Weights ◽  
Equilibrium Sedimentation ◽  
Hemoglobin Molecule ◽  
Ph Range

The molecular weights of horse hemoglobin, horse globin, and performic acid oxidized horse globin were determined by osmotic pressure, by an approach to equilibrium sedimentation, and by light scattering (except hemoglobin) at pH 1.5 to 2.5 in 0.05 M NaCl. Sedimentation coefficients were determined for these materials over the same pH range and electrophoretic analyses were made from pH 1.5 to 4.0. The results show that in dilute salt solutions below pH 2.5 horse hemoglobin dissociates to four subunits all approximately equal in mass but at least two of which differ electrokinetically and therefore in composition. The subunits are probably held together in the native hemoglobin molecule only by non-covalent bonds.

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