scholarly journals Separation of acidic amino-acids by means of a synthetic anion exchange resin

1948 ◽  
Vol 42 (3) ◽  
pp. 443-447 ◽  
Author(s):  
R. Consden ◽  
A. H. Gordon ◽  
A. J. P. Martin
Keyword(s):  
Amino Acids ◽  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Acidic Amino Acids

THE CHROMATOGRAPHIC DETERMINATION OF GLUTAMIC, ASPARTIC, AND CYSTEIC ACIDS USING AN ANION EXCHANGE RESIN

1957 ◽  
Vol 35 (1) ◽  
pp. 1249-1258
Author(s):  
A. M. Marko
Keyword(s):  
Amino Acids ◽  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Chromatographic Determination ◽  
Acetate Buffer ◽  
Cysteic Acid ◽  
Acidic Amino Acids ◽  
Normal Urine ◽  
Dowex 1

Optimum conditions for the separation of the acidic amino acids glutamic, aspartic, and cysteic on an anion exchange resin, Dowex-1 × 8, have been studied. The sample to be analyzed is adjusted to pH 7 and placed on a column of Dowex-1 × 8 previously equilibrated with 0.1 M acetate buffer at pH 4. Glutamic and aspartic acids are separated by elution with 0.1 M acetate buffer at pH 4.0–4.6. Cysteic acid is eluted with 0.2 M acetate buffer at pH 5.5–5.9. With this method quantitative separation of synthetic mixtures of the acidic amino acids has been achieved. This method has also been used to determine the dicarboxylic amino acids in acid hydrolyzates of various proteins, of normal protein-free plasma, and of normal urine.

THE CHROMATOGRAPHIC DETERMINATION OF GLUTAMIC, ASPARTIC, AND CYSTEIC ACIDS USING AN ANION EXCHANGE RESIN

1957 ◽  
Vol 35 (12) ◽  
pp. 1249-1258 ◽  
Author(s):  
A. M. Marko
Keyword(s):  
Amino Acids ◽  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Chromatographic Determination ◽  
Acetate Buffer ◽  
Cysteic Acid ◽  
Acidic Amino Acids ◽  
Normal Urine ◽  
Dowex 1

Optimum conditions for the separation of the acidic amino acids glutamic, aspartic, and cysteic on an anion exchange resin, Dowex-1 × 8, have been studied. The sample to be analyzed is adjusted to pH 7 and placed on a column of Dowex-1 × 8 previously equilibrated with 0.1 M acetate buffer at pH 4. Glutamic and aspartic acids are separated by elution with 0.1 M acetate buffer at pH 4.0–4.6. Cysteic acid is eluted with 0.2 M acetate buffer at pH 5.5–5.9. With this method quantitative separation of synthetic mixtures of the acidic amino acids has been achieved. This method has also been used to determine the dicarboxylic amino acids in acid hydrolyzates of various proteins, of normal protein-free plasma, and of normal urine.

scholarly journals Separation of O-Phosphorylated Amino Acids and Peptides on Anion Exchange Resin.

1959 ◽  
Vol 13 ◽  
pp. 1787-1790 ◽  
Author(s):  
Lars Strid ◽  
Salo Gronowitz ◽  
Sigvard Eriksson ◽  
C.-G. Hedén ◽  
B. Malmgren ◽  
...  
Keyword(s):  
Amino Acids ◽  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin

Isolation of κ-casein glycomacropeptide from bovine whey fraction using food grade anion exchange resin and chitin as an adsorbent

2020 ◽  
Vol 87 (1) ◽  
pp. 127-133 ◽  
Author(s):  
Takuo Nakano ◽  
Mirko Betti
Keyword(s):  
Amino Acids ◽  
Sialic Acid ◽  
Anion Exchange ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Binding Capacity ◽  
Dry Weight ◽  
Food Grade ◽  
Three Samples ◽  
Phosphorylated Peptide

AbstractBovine κ-casein glycomacropeptide (GMP) found in cheese whey is a sialylated phosphorylated peptide which is thought to be a potential ingredient for functional food as well as dietetic food. This study was undertaken to determine whether high purity GMP can be isolated from soluble whey fraction (SWF) using column chromatography on food grade anion exchange resin and chitin as an adsorbent. Samples of commercially available anion exchange resin (resin A, resin B and resin C) and those of chitin (chitin A, chitin B and chitin C) were examined in this experiment. The GMP fraction obtained from each column was analyzed for amino acid composition which reflects the purity of the peptide. Major findings for commercial anion exchange resin were that: (1) the proportion of GMP monitored as sialic acid in total recovered sialic acid was similar among the three samples of resin accounting for average 78% of recovered sialic acid; (2) the GMP fraction from resin A or resin B contained undetectable level of contaminating amino acids including phenylalanine, histidine, arginine and tyrosine; (3) the GMP fraction from resin C contained small amounts (<1 mol%) of contaminating amino acids, arginine, phenylalanine and tyrosine; and (4) the GMP binding capacity expressed as mg/100 mg dry weight of resin was more than 2.5 times higher in resin C (average 22.9) than in resin A or resin B with no difference between resin A and resin B averaging 8.7. Results obtained for chitin A, chitin B and chitin C were in general similar to those found with resin A and resin B. Since chitin has a remarkable GMP binding capacity averaging 8.6 mg/100 mg dry weight of chitin, it may be a useful adsorbent for whey fractionation. Further research is needed to develop an efficient inexpensive method to purify GMP.

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