Ion-exchange chromatography of sulfur amino acids and the separation of diastereoisomers

1963 ◽  
Vol 10 ◽  
pp. 439-442 ◽  
Author(s):  
George W. Frimpter ◽  
Shinji Ohmori ◽  
Shunzi Mizuhara
2014 ◽  
Vol 14 (1-2) ◽  
pp. 151-155
Author(s):  
Wiesław Tadeusiak ◽  
Eliza Balicka

Concentration of free amino acids in the following bracket fungi: <i>Climacodon septentrionalis</i> (Fr) P. Karst, <i>Hapalopilus croceus</i> (Pers. ex Fr.) Donk., <i>Laetiporusus sulphurens</i> (Bull. ex Fr.) Murill and <i>Polyporus squamosus</i> Huds ex Fr., were determined by ion-exchange chromatography.


1969 ◽  
Vol 52 (5) ◽  
pp. 981-984 ◽  
Author(s):  
J E Knipfel ◽  
D A Christensen ◽  
B D Owen

Abstract Amino acid analyses were performed on samples of blood, liver tissue, loin muscle, and ham muscle by ion exchange chromatography after deproteination of the samples with picric acid or sulfosalicylic acid (SSA). Resolution of threonine and serine from the ion exchange column was poor when SSA was used as the deproteinating agent. Twelve of sixteen amino acids were higher (P &lt; 0.05) in serum deproteinated with picric acid as compared to concentrations determined after SSA deproteination. Amino acid values for ham muscle tended to be higher after deproteination with picric acid; however, with liver and loin muscle samples, the values were somewhat higher after SSA deproteination. In both serum and tissue analyses, coefficients of variation were lower for niGSt amino acids when picric acid was utilized as the deproteinating agent. The latter observation, in particular, suggests that picric acid is preferable to SSA as a deproteinating agent before amino acid analyses of biological fluids. Standardization of methods of deproteination is needed to allow meaningful comparisons of data.


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