Quantitative Electrophoresis of Serum Proteins on Paper

1956 ◽  
Vol 2 (5) ◽  
pp. 303-319 ◽  
Author(s):  
Moses Wurm ◽  
Frederick H Epstein
Keyword(s):  
Protein Concentration ◽  
Moving Boundary ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Bromphenol Blue ◽  
Good Resolution ◽  
Confidence Limits ◽  
Protein Patterns ◽  
Electrophoretic Patterns ◽  
Normal Human

Abstract 1. A procedure for paper electrophoresis has been described which gives highly reproducible protein patterns with good resolution and freedom from distortions. 2. Densitometry of protein bands on paper stained with bromphenol blue or Amidoschwarz 10B reveals that the logarithm of protein concentration is proportional to optical density and that Beer's law does not apply. Electrophoretic patterns of normal human serum evaluated in this manner give values in close agreement with those obtained by moving-boundary electrophoresis. 3. Confidence limits were determined for both methods.

Some of the Variables Involved in the Fractionation of Serum Proteins by Paper Electrophoresis

1957 ◽  
Vol 3 (1) ◽  
pp. 49-64 ◽  
Author(s):  
Richard J Henry ◽  
Orville J Golub ◽  
Charles Sobel
Keyword(s):  
Serum Proteins ◽  
Normal Values ◽  
Paper Electrophoresis ◽  
Bromphenol Blue

Abstract Investigation of various steps involved in separation of serum proteins by paper electrophoresis and their quantitation by dyeing with bromphenol blue has revealed that the results obtained are quite dependent on a number of variables. It is essential, therefore, that rigid control of these variables be exercised and that normal values be obtained by the specific technic adopted. Normal values have been given for the technic employed and data on stability of sera at room and refrigerator temperatures have been presented.

Nonionic Surfactants in Paper Electrophoresis

1960 ◽  
Vol 6 (5) ◽  
pp. 413-420 ◽  
Author(s):  
W Donald Graham
Keyword(s):  
Blood Serum ◽  
Nonionic Surfactants ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Protein Levels ◽  
Disease States ◽  
Electrophoretic Patterns ◽  
Blood Serum Proteins ◽  
Number Of Patients ◽  
Γ Globulins

Abstract 1. A modification of the usual paper electrophoretic procedure has been made by including in the buffer medium 0.05 per cent of certain alkylphenyl ethers of polyethylene glycol. 2. This modified procedure yields electrophoretic patterns of blood serum proteins that may be subdivided into 12 fractions— albumin, α1-globulin, three α2-globulins, three β-globulins, and four γ-globulins. 3. The method was applied to blood serum from 70 patients apparently free of significant disease and to sera from a number of patients with varied disease. More specific location of the altered protein levels was possible in a number of disease states. 4. Glycoprotein distribution was not seriously disturbed by the presence of the nonionic surfactants, but lipoproteins migrated at a decreased rate.

Variability in Paper Electrophoretic Patterns of the Serum of Landlocked Sea Lamprey, Petromyzon marinus Linnaeus

1964 ◽  
Vol 21 (2) ◽  
pp. 239-246 ◽  
Author(s):  
M. L. H. Thomas ◽  
H. R. McCrimmon
Keyword(s):  
Life History ◽  
Protein Concentration ◽  
Petromyzon Marinus ◽  
Paper Electrophoresis ◽  
Sea Lamprey ◽  
Electrophoretic Patterns ◽  
In Captivity ◽  
Phase Variations ◽  
Two Phases ◽  
Parasitic Phase

One hundred and fifty-eight samples of sea lamprey (Petromyzon marinus L.) blood were analyzed using paper electrophoresis at pH 8.6. The specimens were of two phases in lamprey life history, the parasitic phase and pre-spawning phase. Variations in serum protein concentration, positions and sizes of the fractions were associated with the state of life history, sex and disease. Most of the variation between phases of life history was in the dominant fraction, an albumin. There was a decrease in total stainable protein while specimens were starved in captivity. Disease caused several changes in the pattern, the most striking of which was an increase in the size of fraction 6, probably α-globulin.

Albumin-Induced Endocytic Vacuoles in Tetrahymena Pyrijormis

1975 ◽  
Vol 33 ◽  
pp. 694-695
Author(s):  
L. J. Brenner ◽  
D. G. Osborne ◽  
B. L. Schumaker
Keyword(s):  
Electron Microscopy ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Tetrahymena Pyriformis ◽  
Sequence Of Events ◽  
Cytoplasmic Bodies ◽  
Food Vacuoles ◽  
Mouse Ascites ◽  
Normal Human

Exposure of the ciliate, Tetrahymena pyriformis, strain WH6, to normal human or rabbit sera or mouse ascites fluids induces the formation of large cytoplasmic bodies. By electron microscopy these (LB) are observed to be membrane-bounded structures, generally spherical and varying in size (Fig. 1), which do not resemble the food vacuoles of cells grown in proteinaceous broth. The possibility exists that the large bodies represent endocytic vacuoles containing material concentrated from the highly nutritive proteins and lipoproteins of the sera or ascites fluids. Tetrahymena mixed with bovine serum albumin or ovalbumin solutions having about the same protein concentration (7g/100 ml) as serum form endocytic vacuoles which bear little resemblance to the serum-induced LB. The albumin-induced structures (Fig. 2) are irregular in shape, rarely spherical, and have contents which vary in density and consistency. In this paper an attempt is made to formulate the sequence of events which might occur in the formation of the albumin-induced vacuoles.

Monoamine Oxidase and Other Mitochondrial Enzymes in Density Subpopulations of Human Platelets

1988 ◽  
Vol 59 (01) ◽  
pp. 029-033 ◽  
Author(s):  
K G Chamberlain ◽  
D G Penington
Keyword(s):  
Monoamine Oxidase ◽  
Protein Concentration ◽  
Close Correlation ◽  
Human Platelets ◽  
Mitochondrial Enzymes ◽  
Density Fractions ◽  
Percoll Gradients ◽  
Normal Human ◽  
The Mean ◽  
Very High

SummaryNormal human platelets have been separated according to density on continuous Percoll gradients and the platelet distribution divided into five fractions containing approximately equal numbers of platelets. The mean volumes and protein contents of the platelets in each fraction were found to correlate positively with density while the protein concentration did not differ significantly between the fractions. Four mitochondrial enzymes (monoamine oxidase, glutamate dehydrogenase, cytochrome oxidase and NADP-dependent isocitrate dehydrogenase) were assayed and their activities per unit volume were found to increase in a very similar monotonie fashion with platelet density. When MAO and GDH were assayed on the same set of density fractions the correlation between the two activities was very high (r = 0.94–1.00, p <0.001) and a similar close correlation was found between MAO and ICDH. The results support the hypothesis that high density platelets either have a higher concentration of mitochondria or have larger mitochondria than low density platelets.

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