The use of cysteic acid as an internal standard in amino acid analysis

1965 ◽  
Vol 20 ◽  
pp. 143 ◽  
Author(s):  
A. Wainer ◽  
J.S. King
2019 ◽  
Author(s):  
Amanda Blake

This protocol describes the deproteinization process that all canine and feline serum and plasma research samples undergo prior to amino acid analysis with a Biochrom 30+ Amino Acid Analyzer at the Gastrointestinal Lab, Texas A&M University. L-norleucine is used as an internal standard.


Vaccine ◽  
2020 ◽  
Vol 38 (29) ◽  
pp. 4507-4511
Author(s):  
Gengcheng J. Yang ◽  
Yanhong Yang ◽  
Andrew Shaddeau ◽  
Cindy X. Cai ◽  
Yile Li ◽  
...  

1971 ◽  
Vol 121 (3) ◽  
pp. 453-459 ◽  
Author(s):  
L. R. Croft ◽  
S. G. Waley

The amino acid sequences around the cysteine residues in the lens protein, γ-crystallin, were studied. Fraction II of the γ-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.


1980 ◽  
Vol 33 (5) ◽  
pp. 513 ◽  
Author(s):  
PH Leighton ◽  
WK Fisher ◽  
KE Moon ◽  
EOP Thompson

Amino acid analysis of oxidized or reduced and carboxymethylated p-glucuronidase have shown the presence of 24 cysteic acid or S-carboxymethylcysteine residues respectively per mole of the tetrameric enzyme. Titration of sulfhydryl groups gave eight cysteine residues, and by difference 16 half-cystine residues per mole.


2012 ◽  
Vol 108 (S2) ◽  
pp. S298-S305 ◽  
Author(s):  
Shane M. Rutherfurd ◽  
Paul J. Moughan

Available amino acids are those absorbed from the gastrointestinal tract in a form suitable for body protein synthesis. True ileal digestible amino acids are determined based on the difference between dietary amino acid intake and unabsorbed dietary amino acids at the terminal ileum. The accuracy of ileal digestible amino acid estimates for predicting available amino acid content depends on several factors, including the accuracy of the amino acid analysis procedure. In heat processed foods, lysine can react with compounds to form nutritionally unavailable derivatives that are unstable during the hydrochloric acid hydrolysis step of amino acid analysis and can revert back to lysine causing an overestimate of available lysine. Recently, the true ileal digestible reactive (available) lysine assay based on guanidination has provided a means of accurately determining available lysine in processed foods. Methionine can be oxidised during processing to form methionine sulphoxide and methionine sulphone and cysteine oxidised to cysteic acid. Methionine sulphoxide, but not methionine sulphone or cysteic acid, is partially nutritionally available in some species of animal. Currently, methionine and cysteine are determined as methionine sulphone and cysteic acid respectively after quantitative oxidation prior to acid hydrolysis. Consequently, methionine and cysteine are overestimated if methionine sulphone or cysteic acid are present in the original material. Overall, given the problems associated with the analysis of some amino acids in processed foodstuffs, the available amino acid content may not always be accurately predicted by true ileal amino acid digestibility estimates. For such amino acids specific analytical strategies may be required.


1975 ◽  
Vol 64 (2) ◽  
pp. 588-592 ◽  
Author(s):  
Roger W. Giese ◽  
James F. Riordan

1988 ◽  
Vol 71 (6) ◽  
pp. 1172-1175
Author(s):  
Ghulam Sarwar ◽  
Herbert G Botting ◽  
Robert W Peace

Abstract The amino acid analysis method using precolumn phenylisothiocyanate (PITC) derivatization and liquid chromatography was modified for accurate determination of methionine (as methionine sulfone), cysteine/cystine (as cysteic acid), and all other amino acids, except tryptophan, in hydrolyzed samples of foods and feces. A simple liquid chromatographic method (requiring no derivatization) for the determination of tryptophan in alkaline hydrolysates of foods and feces was also developed. Separation of all amino acids by liquid chromatography was completed in 12 min compared with 60-90 min by ion-exchange chromatography. Variation expressed as coefficients of variation (CV) for the determination of most amino acids in the food and feces samples was not more than 4%, which compared favorably with the reproducibility of ion-exchange methods. Data for amino acids and recoveries of amino acid nitrogen obtained by liquid chromatographic methods were also similar to those obtained by conventional ion-exchange procedures.


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