Paper Chromatography of Amino Acid

Author(s):  
Aakanchha Jain ◽  
Richa Jain ◽  
Sourabh Jain
1972 ◽  
Vol 1 (4) ◽  
pp. 269-272
Author(s):  
Isamu Akiyama ◽  
Masaji Onaya ◽  
Akira Hayakawa ◽  
Yojiro Tsuzuki

1963 ◽  
Vol 41 (1) ◽  
pp. 1065-1072 ◽  
Author(s):  
R. A. Anwar ◽  
C. Roy ◽  
R. W. Watson

Four closely related uridine nucleotide-peptides isolated from ethanol extracts of penicillin-treated Aerobacter cloacae NRC 492 have been partially characterized. Fractionation of dialyzed extracts on Dowex-1-Cl columns with aqueous lithium chloride solutions, precipitation of the nucleotide-peptides with methanol–acetone, and further separation by paper chromatography and high voltage electrophoresis yielded (a) UDP-GNAc-lact.L-ala.D-glu.meso-dap.D-ala,* (b) UDP-GNAc-lact.L-ala.D-glu.meso-dap, (c) UDP-GNAc-lact.L-ala.D-glu., and (d) UDP-GNAc-lactic acid. The amino acid isomers were identified by micro-enzymic and chromatographic methods.


1952 ◽  
Vol 30 (3) ◽  
pp. 246-249
Author(s):  
I. W. Coleman

An apparatus for the preparation of protein-free filtrates of biological fluids for subsequent amino-acid analysis by paper chromatography is described. The construction allows filtration to be carried out at high pressures, hence increasing the rate of filtration. Contamination by interfering heavy metal ions is avoided by a design in which solutions are exposed only to lucite.


1959 ◽  
Vol 31 (6) ◽  
pp. 1028-1031 ◽  
Author(s):  
J. F. Thompson ◽  
C. J. Morris ◽  
R. K. Gering

1956 ◽  
Vol 21 (4) ◽  
pp. 477-480 ◽  
Author(s):  
S. GHOSH MAJUMDER ◽  
RABINDRA NATH DUTTA ◽  
N. C. GANGULI

1973 ◽  
Vol 26 (4) ◽  
pp. 877 ◽  
Author(s):  
RG Whittaker ◽  
WK Fisher ◽  
EOP Thompson

The amino acid sequence of the 141 residues of the IX-chain of the major haemoglobin (Hb-IB) from the echidna has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, paper ionophoresis, and paper chromatography.


1976 ◽  
Vol 29 (2) ◽  
pp. 73 ◽  
Author(s):  
AR Nash ◽  
WK Fisher ◽  
EOP Thompson

The amino acid sequence of the a-chain of the principal haemoglobin from the shark, H. portusjacksoni has been determined. The chain has 148 residues and is acetylated at the amino terminal. The soluble peptides obtained by tryptic and chymotryptic digestion of the protein or its cyanogen bromide fragments were isolated by gel filtration, paper ionophoresis and paper chromatography. The amino acid sequences were determined by the dansyl-Edman procedure. The insoluble 'core' peptide from the tryptic digestion contained 34 residues and required cleavage by several proteases before the sequence was established. Compared with human a-chain there are 88 amino acid differences including the additional seven residues which appear on the amino terminal of the shark chain. There is also one deletion and one insertion. The chain contains no tryptophan but has four cysteinyl residues which is the highest number of such residues recorded for a vertebrate globin.


1981 ◽  
Vol 46 (3) ◽  
pp. 640-654
Author(s):  
Vladimír Kostka

Aminoethylated hog pepsin was subjected to tryptic digestion and the longest fragment, arising from cleavage at S-(β-aminoethyl)-cysteine residue No II and III was isolated from the digest. This fragment was subjected to additional cleavage with subtilisin and the digest resolved into crude fractions by chromatography on Dowex 1. The isolation and final purification of the peptides was carried out by paper electrophoreses and paper chromatography. By these methods 55 peptides were obtained which were subjected to sequential analysis by stepwise degradation. The amino acid sequences of these peptides and their position in the pepsin chain are given. These sequences provided overlaps for peptides obtained by hydrolysis of this part of the pepsin chain by other enzymes.


1969 ◽  
Vol 15 (9) ◽  
pp. 902-907 ◽  
Author(s):  
William J Culley

Abstract Simple and rapid thin-layer chromatographic methods, using heel or finger-tip blood, are described that are suitable for screening for inborn errors of amino acid metabolism. Serum is chromatographed without deproteinizing. A variation of this method utilizes blood impregnated on paper discs for chromatography. These methods are much faster, more sensitive, and provide better resolution of amino acids than paper chromatography. Because untreated serum- or blood-impregnated discs are placed directly on thin-layer chromatograms, these methods require considerably less working time than other thin-layer chromatographic methods.


1955 ◽  
Vol 25 (4) ◽  
pp. 334-342 ◽  
Author(s):  
R.L. Golden ◽  
J.C. Whitwell ◽  
E.H. Mercer

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