A new abnormal human hemoglobin: Hb prato (α231 (B12) Arg→Ser β2)
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Amino acid substitution
Amino Acid Analysis
A method was developed for quantifying 17 amino acids in tobacco leaves by using an A300 amino acid analyzer and chemometric resolution. In the method, amino acids were eluted by the buffer solution on an ion-exchange column. After reacting with ninhydrin, the derivatives of amino acids were detected by ultraviolet detection. Most amino acids are separated by the elution program. However, five peaks of the derivatives are still overlapping. A non-negative immune algorithm was employed to extract the profiles of the derivatives from the overlapping signals, and then peak areas were adopted for quantitative analysis of the amino acids. The method was validated by the determination of amino acids in tobacco leaves. The relative standard deviations (n = 5) are all less than 2.54% and the recoveries of the spiked samples are in a range of 94.62–108.21%. The feasibility of the method was proved by analyzing the 17 amino acids in 30 tobacco leaf samples.
Amino Acid Analysis
Quantitative Analysis
Chemometrics
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The results of the complex study of the qualitative and quantitative composition of the aminoacids of the grass of three species of the genus Hedysarum growing in the territory of the North Caucasus are presented in the article. The objective of the work is to prepare the comparative aminoacid analysis in three samples of a species of Hedysarum growing in the territory of the North Caucasus. Materials and methods. Qualitative analysis of the amino acid composition was carried out by reaction with ninhydrin, and the quantification of free forms of amino acids was determined by photometric detection at a wavelength of 570 nm on an amino acid analyzer ААА -400. The content of free and bound amino acids was determined after staining the derivatives with ninhydrin and fixing their content at a wavelength of 440 and 570 nm. Analysis of the amino acid composition of these species Hedysarum daghestanicum , Hedysarum caucasicum , Hedysarum grandiflorum is given for the first time. Results. The comparative amino acid composition of the three studied specimens of the Hedysarum genus species growing on the territory of the North Caucasus showed that significant amino acids in the aboveground organs of the studied species were found, such as aspartic and glutamic acids, as well as proline, leucine, and phenylalanine. Conclusion. In conclusion, it should be noted that the bulk of the detected amino acids belongs to the group of essential amino acids, and in addition, the presence of proline and phenylalanine proves the presence of xanthones. The results of the study can be further used in the preparation of a comprehensive metabolic assessment of medicinal plant materials of species of the genus Hedysarum L.
Ninhydrin
Amino Acid Analysis
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Amino acid substitution
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Amino Acid Analysis
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Intra-protein residual vicinities depend on the involved amino acids. Energetically favorable vicinities (or interactions) have been preserved during evolution, while unfavorable vicinities have been eliminated. We describe, statistically, the interactions between amino acids using resolved protein structures. Based on the frequency of amino acid interactions, we have devised an amino acid substitution model that implements the following idea: amino acids that have similar neighbors in the protein tertiary structure can replace each other, while substitution is more difficult between amino acids that prefer different spatial neighbors. Using known tertiary structures for α-helical membrane (HM) proteins, we build evolutionary substitution matrices. We constructed maximum likelihood phylogenies using our amino acid substitution matrices and compared them to widely-used methods. Our results suggest that amino acid substitutions are associated with the spatial neighborhoods of amino acid residuals, providing, therefore, insights into the amino acid substitution process.
Amino acid substitution
Substitution (logic)
Protein tertiary structure
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We developed a simple and rapid method for analyzing nonproteinogenic amino acids that does not require conventional chromatographic equipment. In this technique, nonproteinogenic amino acids were first converted to a proteinogenic amino acid through in vitro metabolism in a cell extract. The proteinogenic amino acid generated from the nonproteinogenic precursors were then incorporated into a reporter protein using a cell-free protein synthesis system. The titers of the nonproteinogenic amino acids could be readily quantified by measuring the activity of reporter proteins. This method, which combines the enzymatic conversion of target amino acids with translational analysis, makes amino acid analysis more accessible while minimizing the cost and time requirements. We anticipate that the same strategy could be extended to the detection of diverse biochemical molecules with clinical and industrial implications.
Amino Acid Analysis
Cell-free protein synthesis
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Amino Acid Analysis
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Abstract Radioactive markers in ion exchange chromatography of amino acid mixtures of biological samples is one of several methods used to identify a particular amino acid. It is shown that in fractions of column effluents-C14-labeled amino acids can be detected relatively easily and economically by liquid scintillation or gas flow systems. The interference of the small quantity of labeled amino acid required to give a significant counting rate with the color yield of the amino acids under investigation has been shown to be negligible.
Ion chromatography
Liquid Scintillation Counting
Amino Acid Analysis
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Amino Acid Analysis
Cardiac muscle
TRACER
Specific activity
Muscle tissue
Muscle protein
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Abstract Intra-protein residual vicinities depend on the involved amino acids. Energetically favorable vicinities (or interactions) have been preserved during evolution, while unfavorable vicinities have been eliminated. We describe, statistically, the interactions between amino acids using resolved protein structures. Based on the frequency of amino acid interactions, we have devised an amino acid substitution model that implements the following idea: amino acids that have similar neighbors in the protein tertiary structure can replace each other, while substitution is more difficult between amino acids that prefer different spatial neighbors. Using known tertiary structures for α -helical membrane (HM) proteins, we build evolutionary substitution matrices. We constructed maximum likelihood phylogenies using our amino acid substitution matrices and compared them to widely-used methods. Our results suggest that amino acid substitutions are associated with the spatial neighborhoods of amino acid residuals, providing, therefore, insights into the amino acid substitution process.
Amino acid substitution
Substitution (logic)
Protein tertiary structure
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