scholarly journals DETERMINATION OF L-ARGININE CONTENT IN SCOTS PINE NEEDLES USING THE SAKAGUCHI TEST

2020 ◽  
pp. 245-254
Author(s):  
Nadezhda Petrovna Chernobrovkina ◽  
Elena Vil'yamovna Robonen ◽  
Kseniya Mikhaylovna Nikerova ◽  
Nataliya Alekseyevna Galibina ◽  
Tamara Nikolayevna Makarova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Optical Absorption ◽  
Spectrophotometric Analysis ◽  
Pine Needles ◽  
Inexpensive Method ◽  
Maximum Extraction ◽  
Coniferous Needles ◽  
Arginine Level ◽  
Scots Pine Needles

Arginine can be accumulated in substantial amounts in coniferous plants whose mineral nutrition is regulated. A simple, quick, accurate and inexpensive method for determining the amino acid in coniferous plant organs is needed to improve the technique of raising the arginine level in the plants and making arginine-rich products of their needles. The aim of this study was to modificate a spectrophotometric method for determining arginine in Pinus sylvestris L. needles containing low or abnormally high levels of the amino acid using the Sakaguchi test. Our studies revealed the agents providing for maximum extraction of arginine from needles. Techniques for stripping the extract of organic compounds and chromogenic reagents for the Sakaguchi test were tested, and the wavelengths of maximum optical absorption of solvents in needle arginine content spectrophotometric analysis were determined. This method is simple, reproducible, accurate, and can be employed to quickly analyze pine needles for arginine content, in particular when developing techniques for augmenting it in coniferous plants and making arginine-rich products of coniferous needles.

The possibility of using Scots pine needles as biomonitor in determination of heavy metal accumulation

2020 ◽  
Vol 27 (16) ◽  
pp. 20273-20280 ◽  
Author(s):  
Houriyah Ateeyah Alwizri Alaqouri ◽  
Cigdem Ozer Genc ◽  
Burak Aricak ◽  
Nadezhda Kuzmina ◽  
Sergey Menshikov ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Scots Pine ◽  
Metal Accumulation ◽  
Heavy Metal Accumulation ◽  
Pine Needles ◽  
Scots Pine Needles

Fully automated liquid-chromatographic determination of amino acids.

1988 ◽  
Vol 34 (12) ◽  
pp. 2510-2513 ◽  
Author(s):  
H M van Eijk ◽  
M A van der Heijden ◽  
C L van Berlo ◽  
P B Soeters
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Daily Practice ◽  
Chromatographic Determination ◽  
Precolumn Derivatization ◽  
Inexpensive Method ◽  
Coefficients Of Variation ◽  
Liquid Chromatographic Determination ◽  
Liquid Chromatographic

Abstract This inexpensive method for fully automated amino acid analysis combines the advantages of automated precolumn derivatization with o-phthaldialdehyde and favorable analytical conditions to separate and quantify 30 amino acids found in normal plasma. The system can run unattended for almost four days, during which the data are processed automatically by a personal computer and a maximum of 76 samples and 19 standards can be processed (cycle time per analysis: 55 min). Only 1 microL of deproteinized plasma is required per analysis. Coefficients of variation for retention times and areas measured for all relevant amino acids are less than 1% and 3%, respectively. The system described is well suited for quick, sensitive operation in daily practice.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

scholarly journals A Method for the Determination of Some Amino Acid Decarboxylases

1960 ◽  
Vol 235 (1) ◽  
pp. 124-127
Author(s):  
Virginia E. Davis ◽  
J. Awapara
Keyword(s):  
Amino Acid

Zur Thermodynamik der hydrophoben Wechselwirkung; die Systeme Wasser + Glycin+ Harnstoff und Wasser + Alanin+ Harnstoff bei 25 °C / Thermodynamics of Hydrophobie Interaction in the Systems Water + Glycin + Urea and Water + Alanin + Urea at 25 °C

1973 ◽  
Vol 28 (9-10) ◽  
pp. 533-554 ◽  
Author(s):  
Lothar Rafflenbeul ◽  
Wa-Ming Pang ◽  
Hansjürgen Schönert ◽  
Klaus Haberle
Keyword(s):  
Amino Acid ◽  
Magnetic Resonance ◽  
Proton Magnetic Resonance ◽  
Pressure Measurements ◽  
Free Enthalpy ◽  
Heat Of Dilution ◽  
Ternary Solutions ◽  
Vapor Pressure Measurements ◽  
Calorimetric Determination

Abstract Isopiestic vapor pressure measurements and calorimetric determination of the heat of dilution have been performed and evaluated with respect to enthalpy, entropy and free enthalpy in the ternary solutions water+ glycin+ urea and water+ alanin + urea. The free enthalpy of transfer for the process: Amino acid from water to water+ urea, which can be derived from these measurements, does not agree with the value calculated from solubility measurements. The reason for this discrepancy and the values of entropy and enthalpy in terms of hydrophobic interaction are discussed. Supplementary measurements of the proton magnetic resonance in these solutions are included.

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.

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