Determination of Amino Acids by Use of Bacterial Amino Acid Decarboxylases

2006 ◽  
pp. 285-306 ◽  
Author(s):  
Ernest F. Gale
Keyword(s):  
Amino Acids ◽  
Amino Acid

scholarly journals Determination of amino acids in human biological fluids by high-performance liquid chromatography: critical review

Amino Acids ◽  
2021 ◽  
Author(s):  
Grażyna Gałęzowska ◽  
Joanna Ratajczyk ◽  
Lidia Wolska
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
High Performance ◽  
Hplc Analysis ◽  
Limit Of Detection ◽  
Biological Fluids ◽  
Analytical Techniques ◽  
Epidemiological Studies ◽  
Preparation Conditions

AbstractThe quantitation and qualification of amino acids are most commonly used in clinical and epidemiological studies, and provide an excellent way of monitoring compounds in human fluids which have not been monitored previously, to prevent some diseases. Because of this, it is not surprising that scientific interest in evaluating these compounds has resurfaced in recent years and has precipitated the development of a multitude of new analytical techniques. This review considers recent developments in HPLC analytics on the basis of publications from the last few years. It helps to update and systematize knowledge in this area. Particular attention is paid to the progress of analytical methods, pointing out the advantages and drawbacks of the various techniques used for the preparation, separation and determination of amino acids. Depending on the type of sample, the preparation conditions for HPLC analysis change. For this reason, the review has focused on three types of samples, namely urine, blood and cerebrospinal fluid. Despite time-consuming sample preparation before HPLC analysis, an additional derivatization technique should be used, depending on the detection technique used. There are proposals for columns that are specially modified for amino acid separation without derivatization, but the limit of detection of the substance is less beneficial. In view of the fact that amino acid analyses have been performed for years and new solutions may generate increased costs, it may turn out that older proposals are much more advantageous.

scholarly journals Determination of Methylated Basic Amino Acids with the Amino Acid Analyzer

1973 ◽  
Vol 248 (7) ◽  
pp. 2387-2391 ◽  
Author(s):  
Gladys E. Deibler ◽  
Russell E. Martenson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Basic Amino Acids ◽  
Amino Acid Analyzer

scholarly journals Determination of free amino acids in plants by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS)

2015 ◽  
Vol 7 (18) ◽  
pp. 7574-7581 ◽  
Author(s):  
Magdalena M. Dziągwa-Becker ◽  
Jose M. Marin Ramos ◽  
Jakub K. Topolski ◽  
Wiesław A. Oleszek
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Tandem Mass Spectrometry ◽  
Free Amino ◽  
Tandem Mass ◽  
Amino Acid Determination ◽  
Acid Determination

Free amino acid determination in plants by LC-MS/MS.

Application of FT-IR Spectrometry to Determine the Global Metabolic Adaptations to Physical Conditioning in Sportsmen

2002 ◽  
Vol 56 (10) ◽  
pp. 1259-1267 ◽  
Author(s):  
Cyril Petibois ◽  
Georges Cazorla ◽  
André Cassaigne ◽  
Gérard Déléris
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ir Spectra ◽  
Plasma Concentrations ◽  
Physical Conditioning ◽  
Ir Spectrometry ◽  
Metabolic Adaptations ◽  
Spectral Area ◽  
Ft Ir

Global metabolic adaptations to physical conditioning were described in 15 subjects by FT-IR spectrometry as the method allowed determination of glucose (Glc), lactate (La), glycerol, triglycerides (TG), fatty acyl moieties (FAM), and total amino acids plasma concentrations. Subtraction of plasma FT-IR spectra obtained at resting state from the exercise spectra also allowed determination of the biomolecular response to exercise. On week 1, exercise induced a transient hypoglycemia, a lactatemia increase of 153%, a FAM depletion of 27%, and a TG concentration decrease of 28%. Protein contents increased by 2%, but these were partly catabolized for amino acid supply (+27%), suggesting an important metabolic stress during exercise. On week 3, exercise hypoglycemia had disappeared, lactate increase was diminished by 91%, TG contents were decreased by 14%, and proteins and amino acids exhibited higher absorption increases. On week 5, TG and FAM concentrations were markedly increased during exercise, protein absorption was still increased (+9%), but amino acid blood release was diminished by 81%. These results described positive adaptations to training. Furthermore, FAM concentration could be determined from plasma FT-IR spectra by using the 2996–2819 cm−1 spectral area [ νas(CH3), νas(CH2), νs(CH3), and νs(CH2) absorbance; 0.82 mMol·L−1, a.u. cm−1], as well as for amino acid concentration by using the ν(COO−) spectral area (1430–1360 cm−1; 0.062 g·L−1, a.u. × cm−1). FT-IR spectrometry was useful to determine simultaneously various plasma concentrations and most of the biomolecular changes through successive samples.

Effect of a Leucine Analogue on Incorporation of Glycine into the Proteins of Explanted Chick Embryos

Development ◽  
1958 ◽  
Vol 6 (2) ◽  
pp. 262-269
Author(s):  
Phyllis W. Schultz ◽  
Heinz Herrmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chick Embryo ◽  
Total Protein ◽  
Nutrient Medium ◽  
Chick Embryos ◽  
Agar Gel ◽  
Egg Extract ◽  
Amino Acid Analogues

Amino acid analogues have been observed to give rise to abnormal forms of development of chick and amphibian embryos (Herrmann, 1953; Rothfels, 1954; Waddington & Sirlin, 1954; Feldman & Waddington, 1955; Herrmann, Rothfels-Konigsberg, & Curry, 1955). Assuming that these disturbances may be due to interference with the utilization of amino acids for protein formation, we have attempted an analysis of this effect by comparison of the protein contents and of the uptake of glycine into the proteins of chick embryo explants in the presence and absence of amino acid analogues. The results of such experiments are reported in this paper. The chick embryos used for explanation, the explantation technique, and the determination of total protein glycine and of tracer glycine were essentially the same as described previously (Herrmann & Schultz, 1958). The embryos were explanted at the 11–13 somite stage on to the surface of an agar gel containing egg extract as nutrient medium following the procedure given by Spratt (1947) as modified by Rothfels (1954).

scholarly journals Comparison of the isotope dilution method for determination of the ileal endogenous amino acid losses with labelled diet and labelled pigs

2000 ◽  
Vol 83 (2) ◽  
pp. 123-130 ◽  
Author(s):  
Vincent Hess ◽  
Philippe Ganier ◽  
Jean-Noel Thibault ◽  
Bernard Sève
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Latin Square ◽  
Isotope Dilution Method ◽  
Dilution Method ◽  
First Case ◽  
Endogenous Protein ◽  
The Individual ◽  
Protein Free Diet

The aims of the present study were first to compare the amino acid dilution method performed using labelled animals with that using labelled diets, and second to determine real digestibilities and total ileal endogenous losses of N and amino acids. Two diets containing pea cultivars (Solara and Amino) and a protein-free diet were compared in a 3 × 3 Latin-square experiment. The three pigs were each prepared with an ileo-rectal anastomosis and were continuously infused with [1-13C]leucine. For each cultivar,15N-labelled and unlabelled diets were formulated. The real digestibility and endogenous losses of leucine were higher when obtained by labelling the pig than by labelling the foodstuff. This was due either to the inadequate estimation of the endogenous protein enrichment in the first case or to the importance of dietary N recycling in the second case. However, in both cases the ileal endogenous losses of N and amino acids were higher than the basal losses determined with the protein-free diet. There were significant differences between the two pea cultivars in terms of phenylalanine and leucine when measured with labelled diets. It is suggested that, although ileal endogenous losses may be underestimated, using labelled feedstuffs is of great interest due to the direct estimation of the individual amounts of amino acids.

Determination of total proteinogenic amino acids and taurine by pre-column derivatisation and UHPLC: Single Laboratory Validation, First Action 2019.09

2020 ◽  
Author(s):  
George Joseph ◽  
Asha Varughese ◽  
Ann Daniel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Infant Formula ◽  
Retention Time ◽  
Sulfonic Acid ◽  
Internal Standard ◽  
The Other ◽  
Method Performance ◽  
Single Laboratory

Abstract Background A method has been developed and validated for selective, accurate and precise determination of total proteinogenic amino acids and taurine from Infant Formula and Adult/Pediatric Nutritional Formulas (powders, ready-to-feed liquids, and liquid concentrates). The method was reviewed by the AOAC INTERNATIONAL SPIFAN Expert Review Panel (ERP) during the 133rd AOAC Annual Meeting & Expo on September 7, 2019 in Denver, CO, USA and was recommended to First Action Official MethodsSM status. Objective The method involves protein hydrolysis to amino acids, a simple pre-column derivatisation of amino acids and separation of derivatised amino acids by UHPLC. The quantification of amino acids is performed by multi-point calibration using norvaline as the internal standard. The analytical method is capable of quantitative determination for 22 proteinogenic amino acids, but cannot be used to quantitate tryptophan, which is destroyed during the acid hydrolysis step. Asparagine is determined as aspartic acid and glutamine as glutamic acid. The cystine and cysteine are converted to S-2-carboxyethylthiocysteine (CYSx) and the derivative is separated from the other amino acids. Citrulline which is present in some matrices and it is separated from other amino acids is not included in the method performance evaluation in the single laboratory validation (SLV). Method The proposed method met all the performance requirement limits set in standard method performance requirements (SMPR) 2014.013 for total proteinogenic amino acids and taurine. The correlation coefficient of multi-point calibration was not less than 0.999 for any amino acids at any point in the SLV study confirming the validity of linear dynanic range (LDR) and linearity of the method. The individual amino acids in the chromatogram were identified by absolute retention time and relative retention time (RRT) with respect to the internal standard norvaline. There were no significant (S/N Ratio <10) interferences from the reagents or by-products of derivatisation and targeted matrices. The method demonstrated high selectivity. Result Accuracy of the method was validated using standard reference materials (NIST SRM 1869 and 1849a) and spike recovery studies. The amino acid results in the SRMs were within the ranges of Reference Mass Fraction Values. The accuracy of the method was corroboratively validated by spike recovery studies. The average spike recovery range between 93 to 107% ensure the accuracy of the method for amino acids and compliance to the AOAC SMPR 2014.013. Conclusions Precision data of the method demonstrate that it meets the stakeholder requirements as per the SMPR. The mean RSDr for all the amino acids for 17 matrices selected for the SLV were not more than 4%. The method is very sensitive and the LOQ can go down to approximately ten times lower than the SMPR requirements. The sensitivity of method is a direct reflection of its signal to noise ratio which ensures guaranteed method performance at the lower levels of amino acids in these matrices. Highlights Taurine (aminoethane sulfonic acid) unlike the other amino acids is a beta-sulfonic amino acid that is not used in protein synthesis but is found as a free amino acid in tissues. The acidic functional group (-COOH) in common amino acid is replaced with a sulfonic acid (-SO3H) group in Taurine. The method offers baseline separation of citrulline which is an alpha amino acid generally present in Infant Formula and Adult/Pediatric Nutritional products. The separation of citrulline eliminates the risk of interference of this compound with other amino acids. The method can also separate and quantitate hydroxyproline, an important component of collagen that is often used to quantitate collagen. The method is simple and does not include any proprietary chemicals or instruments and can be performed on any basic reverse phase UHPLC system with UV detection.

The Oocytes of the Goby Pomatoschistus minutus. III. Determination of Amino Acid Component

1980 ◽  
Vol 35 (11-12) ◽  
pp. 1094-1095
Author(s):  
Rüdiger Riehl
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Acid Component ◽  
Pomatoschistus Minutus ◽  
Protein Amino Acids ◽  
Amino Acid Component

Abstract The oocytes of the marine goby Pomatoschistus minutus were analyzed for their amino acid content. Most of the amino acids exist as protein, only a little part is free or peptide-bound. Among the protein-bound amino acids, high levels of glutamic acid, proline, alanine, aspartic acid, valine and leucine were detected. These represent more than 60% of the protein amino acids. Among the free acids, glutamic acid, serine and alanine, are dominant. There are no certain proofs of the occurrence of peptide pools in the oocytes of Pomatoschistus minutus.

An Automated Detection System for Most L-α-Amino Acids

1969 ◽  
Vol 15 (2) ◽  
pp. 154-161 ◽  
Author(s):  
K Van Dyke ◽  
C Szustkiewicz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Detection System ◽  
Automated System ◽  
Acid Oxidase ◽  
Enzymatic Reactions ◽  
Amino Acid Oxidase ◽  
Automated Method ◽  
Wide Range

Abstract An automated system for the determination of the L-α form of the majority of amino acids is presented. The method is based upon oxidative deamination of the amino acid coupled with oxidation of o-dianisidine by hydrogen peroxide. This procedure can be used comparatively for the determination of a mixture of L-α-amino acids or for the majority of separated L-α-amino acids (especially in conjunction with column separations from urine and blood which give falsely positive identification with ninhydrin detection). The stereospecific nature of the L-α-amino acid oxidase enables the investigator to quantitate the amount of L-α-amino acid in the presence of the D-α form. From an academic viewpoint, the extreme sensitivity and wide range of the detection system make it advantageous for the study of the enzyme itself. This automated method also may be employed to follow enzymatic reactions—e.g., those catalyzed by peptidases or racemases. The methodology is extremely convenient with good reagent stability and is much more sensitive than manometric technics.

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