PAPER CHROMATOGRAPHY OF COMPLEX BIOLOGICAL MATERIALS BY SOLVENT REDEVELOPMENT WITHOUT PRIOR REMOVAL OF SALTS OR PROTEINS

1960 ◽  
Vol 38 (10) ◽  
pp. 1137-1147 ◽  
Author(s):  
Arthur E. Pasieka

A solvent redeveloping technique has been devised by which amino acids, peptides, and sugars can be separated from complex mixtures in the presence of high concentrations of salts and proteins. The separations are effected by two to four successive 18-hour solvent developments with drying between each 18-hour period before subsequent staining of the chromatograms. Better separations and resolutions are obtained by such successive 18-hour solvent developments than by one continuous solvent development for an equivalent time. The effect of these redevelopments on the separations and resolutions of biological compounds is illustrated at various stages by photographs of one- and two-dimensional chromatograms. The redevelopment technique requires filter paper sheets up to 4 ft in length for one-dimensional analytical and preparative types of chromatograms.

1960 ◽  
Vol 38 (1) ◽  
pp. 1137-1147 ◽  
Author(s):  
Arthur E. Pasieka

A solvent redeveloping technique has been devised by which amino acids, peptides, and sugars can be separated from complex mixtures in the presence of high concentrations of salts and proteins. The separations are effected by two to four successive 18-hour solvent developments with drying between each 18-hour period before subsequent staining of the chromatograms. Better separations and resolutions are obtained by such successive 18-hour solvent developments than by one continuous solvent development for an equivalent time. The effect of these redevelopments on the separations and resolutions of biological compounds is illustrated at various stages by photographs of one- and two-dimensional chromatograms. The redevelopment technique requires filter paper sheets up to 4 ft in length for one-dimensional analytical and preparative types of chromatograms.


1966 ◽  
Vol 44 (2) ◽  
pp. 149-153 ◽  
Author(s):  
A. E. Pasieka ◽  
J. E. Logan

The use of a solvent redevelopment technique enables the separation of amino acids from complex biological materials in the presence of high concentrations of salts. By conventional chromatography, 1.17 mg of total amino acids have been separated from the high salt medium M 150. The preparative technique as described here has separated amounts as great as 1.17 g and the patterns are essentially the same as for the analytical types. The separations are effected by four or more successive 15- to 20-hour solvent developments with drying between each solvent stage before the staining of chromatograms or isolation of particular bands. The results of these solvent developments on the preparative scale are illustrated with photographs of actual chromatograms. This technique requires thick filter paper sheets up to 4 ft in length for analytical, and particularly for preparative, chromatograms.


1951 ◽  
Vol 23 (1) ◽  
pp. 168-174 ◽  
Author(s):  
E. F. McFarren

1948 ◽  
Vol 1 (1) ◽  
pp. 98 ◽  
Author(s):  
JWH Lugg ◽  
BT Overell

Procedures have been described for "one-" and "two-dimensional" partition-chromatographic separations, on an inert sheet (paper) support, of mixtures of relatively non-volatile organic acids. Ionization, and adsorption of the acids by the paper, have been suppressed by swamping both the stationary and mobile solvent phases with a volatile acid (acetic or formic). Formic acid is superior in that, at high concentration, it permits welldefined bands of the test acids to travel down the sheets and confers upon the bands highly characteristic RF values. RF values for some acids (malic, citric, tartaric, succinic, fumaric, malonic, pyruvic, lactic, ketosuccinic (oxalacetic), α-ketoglutaric, monomethyl succinic, glutaric, and adipic) at 20°C., when Whatman No. 1 filter paper and various pairs of solvent phases are used. have been provided. Some of the acids present in carrot tissue have been separated in "one-dimensional" work and identified by their RF values.


1970 ◽  
Vol 16 (8) ◽  
pp. 662-666 ◽  
Author(s):  
F Kraffczyk ◽  
R Helger ◽  
H Lang

Abstract Separation of the amino acids in urine by use of thin-layer chromatography (TLC) has hitherto required that the specimen be first desalted and then chromatographed in two dimensions with at least two pairs of developing solvent systems. We wished to simplify both steps. The customary method of desalting on a column is replaced by desalting on a plate that supports a strongly acid cation-exchanger and a cellulose layer. This method, originally developed for one-dimensional TLC, is used here for two-dimensional TLC. Urine is applied to the ion-exchange layer and strong acids and neutral substances are removed with water. The amino acids are then chromatographed into the cellulose layer, and are separated there two dimensionally with a newly devised pair of developing solutions. This pair of solvents separates nearly all of the amino acids in urine.


1957 ◽  
Vol 3 (5) ◽  
pp. 721-728 ◽  
Author(s):  
F. Reusser ◽  
J. F. T. Spencer ◽  
H. R. Sallans

The cells of 19 species of bacteria, actinomyces, and yeasts were analyzed for protein and essential amino acids. A rapid quantitative method for amino acid determination using one-dimensional paper chromatography was developed. The cellular protein from all species contained relatively high concentrations of lysine, somewhat lower concentrations of tryptophan and threonine, and very low concentrations of methionine. All of the 10 essential amino acids were found in each species tested, although individual differences in the relative and absolute amounts were observed.


Science ◽  
1951 ◽  
Vol 113 (2923) ◽  
pp. 4-6 ◽  
Author(s):  
M. K. Brush ◽  
R. K. Boutwell ◽  
A. D. Barton ◽  
C. Heidelberger

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