scholarly journals NMR spectroscopy of Cu(II) complexes with acrylamide and sodium acrylate copolymer and ω-amino acids

2021 ◽  
pp. 85-98
Author(s):  
Дмитрий Леонович Кудрявский ◽  
Елена Константиновна Фомина ◽  
Людмила Юльевна Тычинская ◽  
Евгений Доминикович Скаковский ◽  
Светлана Евгеньевна Богушевич
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Aminocaproic Acid ◽  
Aminobutyric Acid ◽  
Molar Ratio ◽  
Sodium Acrylate ◽  
Amino Groups ◽  
Acrylate Copolymer ◽  
Carboxylic Groups

Macromolecular complexes of acrylamide and sodium acrylate copolymer with microelements, including Cu(II), may form at preparation of crop protection and stimulation compositions, where the copolymer serves as an adhesive, water-retaining and film-forming agent. Preparations for crop production may also contain amino acids that protect plants under stressful conditions (cold, dry, etc.). Carboxylic groups of copolymer, carboxylic and amino groups of amino acids may be involved in mixed Cu(II) ions complexes formation. Number of methylene groups separating carboxylic and amino group of amino acids affects its ability to form a stable chelate cycle and, therefore, ligand composition of mixed Cu(II) ions complexes with acrylamide and sodium acrylate copolymer and amino acid. This work is aimed at determining the ligand composition of mixed macromolecular Cu(II) ion complexes with acrylamide and sodium acrylate copolymer and ω-amino acids (β-alanine, γ-aminobutyric acid, ε-aminocaproic acid). 13C and 1H NMR spectroscopy was used to clarify complexes composition. A complex where carboxylic groups of amino acids are ligands has been found to form in aqueous solutions of Cu(II) ions and ω-amino acid (β-alanine, γ-aminobutyric acid, ε-aminocaproic acid) at molar ratio of Cu(II) ions – amino acid equal to 1 : 6. A chelate complex where both carboxylic and amino groups of β-alanine are involved in coordination has been discovered to form in the solution containing Cu(II) ions, β-alanine, as well as acrylamide and sodium acrylate copolymer at molar ratio of Cu(II) – β-alanine – copolymer COO− equal to 1 : 6 : 30. Carboxylic groups of copolymer participate in complex formation as well. Carboxylic groups of both amino acids and the copolymer have been shown to participate in complex formation in aqueous solutions containing Cu(II) ions, either γ-aminobutyric or ε-aminokaproic acid and also acrylamide and sodium acrylate copolymer.

Purification of Antihemophilic Factor (Factor VIII) by Amino Acid Precipitation*

1964 ◽  
Vol 11 (01) ◽  
pp. 064-074 ◽  
Author(s):  
Robert H Wagner ◽  
William D McLester ◽  
Marion Smith ◽  
K. M Brinkhous
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Factor Viii ◽  
Plasma Protein ◽  
Acid Precipitation ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid ◽  
Specific Procedure ◽  
Beta Alanine ◽  
Antihemophilic Factor

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.

Extent of damage to amino acid availability of whey protein heated with sugar

1991 ◽  
Vol 58 (4) ◽  
pp. 431-441 ◽  
Author(s):  
Thérèse Desrosiers ◽  
Laurent Savoie
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Whey Protein ◽  
Significant Proportion ◽  
Protein Digestibility ◽  
Heating Time ◽  
Heat Treatments ◽  
Molar Ratio ◽  
Amino Acid Availability

SummaryThe effect of heat treatments, at various water activities (αw), on digestibility and on the availabilities of amino acids of whey protein samples in the presence of lactose was estimated by an in vitro digestion method with continuons dialysis. Four αw (0·3, 0·5, 0·7 and 0·97), three temperatures (75, 100 and 121 °C) and three heating periods (50, 500 and 5000 s) were selected. The initial lysine: lactose molar ratio was 1:1. Amino acid profiles showed that excessive heating of whey (121 °C, 5000 s) destroyed a significant proportion of cystine at all αw, lysine at αw 0·3, 0·5 and 0·7, and arginine at αw 0·5 and 0·7. At αw 0·3, 0·5 and 0·7, protein digestibility decreased (P < 0·05) as the temperature increased from 75 to 121 °C for a heating period of 5000 s, and as the heating time was prolonged from 500 to 5000 s at 121 °C. Excessive heating also decreased (P < 0·05) the availabilities of ail amino acids at αw 0·3, 0·5 and 0·7. The availabilities of lysine, proline, aspartic acid, glutamic acid, threonine, alanine, glycine and serine were particularly affected. Severe heating at αw 0·97 did not seem to favour the Maillard reaction, but the availabilities of cystine, tyrosine and arginine were decreased, probably as a result of structural modifications of the protein upon heating. Heating whey protein concentrates in the presence of lactose not only affected lysine, but also impaired enzymic liberation of other amino acids, according to the severity of heat treatments and αw.

scholarly journals Quantification By Gas Chromatography of the Content of Amino Acids Present in Sausages Fortified with Quinoa Vegetable Protein

2021 ◽  
Author(s):  
A. Zavala ◽  
M. González ◽  
P. Pino
Keyword(s):  
Amino Acids ◽  
Gas Chromatography ◽  
Amino Acid ◽  
Vegetable Protein ◽  
Amino Acid Profile ◽  
Aminobutyric Acid ◽  
Precolumn Derivatization ◽  
Proportional Relationship ◽  
Quinoa Flour

The objective of this research was to determine the quality of the protein present in sausages fortified with quinoa as a substitute for animal protein, through the identification and quantification of amino acids, using gas chromatography and precolumn derivatization. The amino acid composition found in the analyzed products was predominantly composed of: Threonine (THR) with a concentration of 1046.32µmol / L, aminobutyric acid (ABA) with a concentration of 9685.68 µmol / L and glutamic acid (GLU) with a concentration of 1178.71 µmol / L. These values were found in the treatment with the highest percentage of quinoa flour, establishing a directly proportional relationship between the concentrations of these amino acids and the percentage of quinoa. Gas chromatography was an adequate technique for determining the amino acid profile due to its speed and sensitivity. Keywords: amino acids, sausages, quinoa, derivatization, gas chromatography. RESUMEN La presente investigación tiene por objetivo determinar la calidad de la proteína presente en embutidos fortificados con quinua como sustituyente de la proteína animal, a través de la identificación y cuantificación de aminoácidos mediante la aplicación de cromatografía de gases y la derivatización precolumna. La composición de aminoácidos encontrada en los productos analizados destaca la presencia mayoritaria de: Treonina (THR) con una concentración de 1046,32 µmol/L, ácido aminobutírico (ABA) con una concentración de 9685,68 µmol/L  y ácido glutámico (GLU) con una concentración de 1178,71 µmol/L, todos estos valores se presentaron en el tratamiento con mayor porcentaje de harina de quinua estableciéndose una relación directamente proporcional entre las concentraciones de estos aminoácidos y el porcentaje de adición de quinua en los tratamientos estudiados. Se puede concluir que la cromatografía de gases empleada resultó una técnica adecuada para la determinación del perfil aminoacídico por la rapidez y sensibilidad presentada sobre las muestras estudiadas.  Palabras claves: aminoácidos, embutidos, quinua, derivatización, cromatografía de gases.  

Radiation Damage to Polypeptides and Proteins in the Solid State: Changes in Amino Acid Composition *

1981 ◽  
Vol 36 (3-4) ◽  
pp. 310-318 ◽  
Author(s):  
J. Seredynski ◽  
T. Söylemez ◽  
W. Baumeister
Keyword(s):  
Amino Acids ◽  
Electron Microscope ◽  
Amino Acid ◽  
Solid State ◽  
Trypsin Inhibitor ◽  
Concanavalin A ◽  
Thin Layers ◽  
Aminobutyric Acid ◽  
Sensitivity Pattern ◽  
State Changes

Thin layers of synthetic homopolypeptides (poly-α-Ala, -Arg, -Asn, -Asp, -Glu, -His, -Lys and -Tyr) and proteins (myoglobin, concanavalin A, trypsin-inhibitor) were irradiated under solid state conditions in an electron microscope with 100 keV electrons. Radiolytic changes were investigated by amino acid analysis. The results are discussed in terms of the relative radiosensitivities of the constituent amino acids, and possible topochemical effects on the sensitivity pattern emerging. An attempt is also made to trace at least some of the predominant pathways of amino acid transformation, namely the production of alanine and a-aminobutyric acid

In Vitro adsorption Spectrum of Plasma Amino Acids by Coated Charcoal Hemoperfusion

1983 ◽  
Vol 6 (5) ◽  
pp. 267-270 ◽  
Author(s):  
Z.Q. Shi ◽  
T.M.S. Chang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Hepatic Coma ◽  
Aromatic Amino Acids ◽  
Molar Ratio ◽  
Adsorption Experiment ◽  
Preferential Adsorption ◽  
Branched Chain ◽  
Charcoal Hemoperfusion

In order to clarify wether coated charcoal hemoperfusion is capable of normalizing amino acid disturbances in hepatic coma, in vitro adsorption and in vitro hemoperfusion studies were carried out. We have found that collodion-coated activated charcoal beads preferentially removed much more aromatic acids (AAA) than branched chain amino acids (BCAA). In the in vitro adsorption experiment with 50 μM amino acid standards aqueous solution, 99% of AAAs were removed by charcoal while only 50 to 81% of BCAAs were removed. As the concentration of amino acids in solution was doubled from μM to 100 μM, BCAA removal was halved while about 90% of AAA was still being removed. In vitro hemoperfusion with heparinized blood from hepatic failure rats, the clearance and the removal of AAAs were significantly greater than those of BCAAs. Consequently, the molar ratio of BCAA over AAA was markedly improved from the initial 1.09 to 3.87 after 60 min of hemoperfusion. Thus, we have demonstrated the preferential adsorption of aromatic amino acids by collodion-coated charcoal beads. The correction of BCAA/AAA molar ratio is also demonstrated.

scholarly journals Determination of Amino Acid Composition of Ganirelix Acetate in an Injectable Formulation by Pre-column Derivatization with 6-Aminoquinolyl-N-hydroxysuccinimidyl Carbamate

2020 ◽  
Vol 58 (8) ◽  
pp. 687-694
Author(s):  
Kumarswamy Ummiti ◽  
J V Shanmukha Kumar
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Flash Chromatography ◽  
Molar Ratio ◽  
Acid Mixture ◽  
Injectable Formulation

Abstract Ganirelix is a synthetic decapeptide linked with nine different amino acids. To understand the peptide amino acid sequence or primary structure, the first step is to determine the amino acid composition of the peptide which can be a determining factor for the peptide immunogenicity. Edman degradation is not a suitable analytical technique to identify amino acid sequence present in Ganirelix due to the absence of uncharged N-terminal amino group. To address this challenge, a pre-column derivatization method was developed with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent. In the present work, the Ganirelix active pharmaceutical ingredient present in the injectable formulation was isolated by fraction collection and further purified by flash chromatography. The amino acid composition of Ganirelix is assayed by carrying out acid hydrolysis with 6 mol L−1 hydrochloric acid solution containing 1% phenol at 100°C for 24 h and derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent solution, followed by determination of individual amino acids by reverse-phase chromatography using a C18 column. High resolution was achieved for the nine amino acid mixture. The amino acid composition results of temperature-stressed Ganirelix generic product and reference listed drug are in good agreement with the theoretical molar ratio of label information.

Variations in the concentrations of free amino acids in the plasma of the dairy cow at parturition

1972 ◽  
Vol 39 (3) ◽  
pp. 355-364 ◽  
Author(s):  
R. Verbeke ◽  
E. Roets ◽  
G. Peeters
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino ◽  
Milk Protein ◽  
Sampling Period ◽  
Aminobutyric Acid ◽  
Amino Acid Utilization ◽  
Amino Acid Levels ◽  
The Mean ◽  
Peak Value

SummaryThe plasma levels of individual amino acids were studied in 6 dairy cows from 4 days before to 3 days after calving. During this sampling period, the concentrations of 13 amino acids showed significant changes. The levels of several amino acids were depressed markedly in the sample collected immediately before calving. Following parturition, the concentration of most amino acids gradually returned to values obtained 3 days before calving. The glutamine and alanine contents of the plasma rose to a peak value 1 day after calving and subsequently decreased. The mean concentrations of glycine and α-aminobutyric acid did not change before parturition but rose significantly thereafter. These observations are discussed in terms of amino-acid utilization for milk protein synthesis and gluconeogenesis at the onset of lactation. The changes in plasma amino acid levels appear to be synchronized with those reported for prolactin and progesterone in the 24 h before parturition. This may indicate an important influence of both hormones on the lactogenic process in the cow. The highly significant correlations obtained between the concentrations of 14 individual amino acids are discussed.

scholarly journals Release of selected amino acids from zinc carriers

2016 ◽  
Vol 66 (2) ◽  
pp. 269-277
Author(s):  
Renata Dyja ◽  
Barbara Dolińska ◽  
Florian Ryszka
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Molar Ratio ◽  
Time Intervals ◽  
Solubility In Water ◽  
First Order ◽  
First Order Kinetics ◽  
Acid Release ◽  
Co Precipitation ◽  
Low Solubility

Abstract The paper deals with the results of an investigation of the release of selected amino acids (histidine, tryptophan, tyrosine) from model suspensions prepared by co-precipitation with zinc chloride. It has been proven that the influence of the Zn(II)/amino acid molar ratio on dissolution profiles of the tested amino acids and dissolution half-life (t1/2) of histidine or tryptophan is significant. The amount of amino acid in the dispersed phase (supporting dose) is a determinant of the amino acid release profile. There is a minimal supporting dose (30.0 μmol of histidine or 17.4 μmol of tryptophan) that provides release of similar amounts of amino acid (4.1–4.6 μmol of histidine or 8.7–9.9 μmol of tryptophan) after the same time intervals. The tyrosine release profiles follow first order kinetics since the supporting dose (0.9–11.2 μmol) is limited by the tyrosine low solubility in water.

Des acides aminés stimulateurs et inhibiteurs à la croissance de Corynebacterium sepedonicum (Spieck. et Kott., Skapt. et Burkh.) dans des milieux synthétiques

1978 ◽  
Vol 24 (9) ◽  
pp. 1087-1092
Author(s):  
G. J. Ikin ◽  
H. J. Hope ◽  
R. A. Lachance
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ammonium Phosphate ◽  
Methionine Sulfoxide ◽  
High Rate ◽  
Molar Ratio ◽  
Corynebacterium Sepedonicum ◽  
Ring Rot ◽  
Acides Aminés ◽  
Synthetic Media

Some aspects of the growth and amino acid metabolism of Corynebacterium sepedonicum, the organism responsible for potato ring rot, have been studied in synthetic media. It has been demonstrated that organic sulfur is required for growth. Methionine supports growth and can be replaced by methionine sulfoxide and cystathionine. Methionine is a micrometabolite for this species as indicated by the fact that optimum growth can be obtained in an asparagines–methionine (asn-met) containing medium when the molar ratio of these amino acids is 56:1. Increasing the proportion of methionine does not increase the growth. Both asparagine and glutamine are metabolized very quickly and provide for equivalent rapid growth unlike aspartic and glutamic acids. In the case of the last two amino acids, growth can be increased if dibasic ammonium phosphate is added to the medium although this compound alone will not support growth in the culture medium. The intracellular soluble asparagine level is extremely low in cells from the asn-met medium indicating a high rate of metabolism compared to aspartic acid. Cystine and cysteine were found to be inhibitory to the organism: they do not affect the rate of uptake of asn or met but do alter the organism's metabolism as reflected by changes in the free amino acid pool. The concentrations of cystine and cysteine required for measurable inhibition are much higher than those found in soluble amino acids of potato tubers.

A convenient preparative method for esters of amino acids

1972 ◽  
Vol 25 (6) ◽  
pp. 1293 ◽  
Author(s):  
JA Maclaren
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Ester ◽  
Preparative Method ◽  
Amino Acid Ester ◽  
Carboxyl Group ◽  
Amino Groups ◽  
Amino Protection

The amino groups of amino acids can be protected by using ethyl ecetoacetate as a ,β-dicarbonyl component. The resulting derivatives are readily alkylated at the carboxyl group by substituted benzyl and other halides. Mild acidolysis then removes the amino protection to give the salt of the amino acid ester. This three-step synthesis can be performed without isolation of intermediates and provides a convenient preparative method for 4-methoxybenzyl, 2,4,6-trimethyl-benzyl, 4-nitrobenzyl, and 4-picolyl esters of amino acids. The products are not racemized.

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