scholarly journals Stability of amino acids and related amines in human serum under different preprocessing and pre-storage conditions based on iTRAQ®-LC-MS/MS

Biology Open ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. bio055020
Author(s):  
Zhuoling An ◽  
Chen Shi ◽  
Pengfei Li ◽  
Lihong Liu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Human Serum ◽  
Large Scale ◽  
Storage Conditions ◽  
Sample Collection ◽  
Serum Samples ◽  
Treatment Measures ◽  
Isobaric Tagging ◽  
Pre Treatment

ABSTRACTAmino acid analysis or metabonomics requires large-scale sample collection, which makes sample storage a critical consideration. However, functional amino acids are often neglected in metabolite stability studies because of the difficulty in detecting and accurately quantifying them with most analysis methods. Here, we investigated the stability of amino acids and related amines in human serum following different preprocessing and pre-storage procedures. Serum samples were collected and subjected to three storage conditions; cold storage (4°C), room temperature storage (22°C), and freezing (−80°C). The concentration of amino acids and related amines were quantified using iTRAQ®-LC-MS/MS with isobaric tagging reagents. Approximately 54.84%, 58.06%, and 48.39% of detectable and target analytes were altered at the 4°C condition, 22°C condition, and when subjected to freeze-thaw cycles, respectively. Some amino acids which are unstable and relatively stable were found. Our study provides detailed amino acid profiles in human serum and suggests pre-treatment measures that could be taken to improve stability.

scholarly journals Stability of amino acids and related amines in human serum under different preprocessing and pre-storage conditions based on iTRAQ®-LC-MS/MS

2020 ◽  
Author(s):  
Zhuoling An ◽  
Chen Shi ◽  
Pengfei Li ◽  
Lihong Liu
Keyword(s):  
Amino Acids ◽  
Human Serum ◽  
Storage Conditions ◽  
Serum Samples ◽  
Freeze Thaw ◽  
Treatment Measures ◽  
Isobaric Tagging ◽  
Pre Treatment ◽  
The Stability ◽  
Immediate Analysis

AbstractAmino acids analysis or metabonomics requires abundant serum/plasma samples collection and samples storage has become inevitable given the limited capacity for immediate analysis. Currently, most of the existing studies on metabolites stability during sample storage focused on long-term and short-term stability, while many functional amino acids might be ignored due to the poor sensitivity and detection of analysis methods. Here, we attempted to elucidate the stability of amino acids and related amines as comprehensive as possible in human serum following different preprocessing and pre-storage procedures. Pooled, fasting serum samples were collected and stored at 4 °C and 22 °C respectively after a delay in sample processing (0, 1, 2, 4, 8, 12 and 24 hours) and underwent freeze-thaw cycles for three times at −80 °C. The concentration of amino acids and related amines were quantified using isobaric tagging reagent iTRAQ®-LC-MS/MS. Approximately 54.84 %, 58.06 % and 48.39 % of detectable and target analytes altered at 4 °C and 22 °C during pre-treatment and freeze-thaw cycles. Some amino acids which are not stable and relatively stable were found. Our study provided detailed profiles and suggestions for amino acids in human serum corresponding to diverse collection and pre-treatment measures.

A SUBCLINICAL BLUETONGUE VIRUS INFECTION IN RUMINANTS WITH THREE UNIQUE AMINO ACID VARIATIONS ON VP7 CORE PROTEIN OF TAIWAN ISOLATES

2019 ◽  
Vol 45 (03) ◽  
pp. 67-77 ◽  
Author(s):  
Jia-Ling Yang ◽  
Lenny Hao-Che Yen ◽  
Well Chia-Wei Yen ◽  
Fun-In Wang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Bluetongue Virus ◽  
Large Scale ◽  
Core Protein ◽  
T Cell Response ◽  
Amino Acid Sequences ◽  
Current Status ◽  
Three Dimensional Model ◽  
Serum Samples

Bluetongue is an arthropod-borne disease in domestic and wild ruminants caused by bluetongue virus (BTV), and it leads to great economic loss worldwide. Previous studies showed that BTV in ruminants in Taiwan was often subclinical infection. The aim of this study was to determine the current status (years 2016–2017) of BTV infection in ruminants in Taiwan, to compare it to the results of a large-scale study conducted in the year 2003, and to investigate whether new viral strains exist. Competitive ELISA tests of serum samples for anti-BTV-VP7 group-specific antibody revealed seropositive rates of 26.7% in cattle by head, similar to 32.7% in the year 2003, suggestive of a BTV-vector-host (cattle) dynamic balance. In goats, the seropositive rate was 18.6%, slightly increased from 8.2% in the year 2003, suggestive of a slow but active infection taking place. This notion was supported by the detection of VP1 gene nucleic acid from whole blood in six out of 29 seropositive goats by reverse transcription–polymerase chain reaction. However, no new virus strain was isolated from embryonating chicken embryos (ECEs) inoculation. Alignment of VP7 amino acid sequences revealed that Taiwan and Japan isolates possessed three specific amino acids on sites No. 82 (arginine), No. 328 (aspartate), and No. 336 (glutamine), which are different from many countries. In a three-dimensional model, these amino acids were located closely on the middle lateral surface of VP7 trimers. Since VP7 is a major outer protein engaged in entry into insect cells and a strong T cell response inducer, these differences likely indicate the result of positive selection of local vectors and hosts in Taiwan.

scholarly journals Free Amino Acids in Peanuts as Affected by Seed Size and Storage Time1

1981 ◽  
Vol 8 (2) ◽  
pp. 113-116 ◽  
Author(s):  
Harold E. Pattee ◽  
Clyde T. Young ◽  
Francis G. Giesbrecht
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Seed Size ◽  
Free Amino Acids ◽  
Free Amino ◽  
Storage Conditions ◽  
Commercial Source ◽  
And Storage

Abstract Peanuts from a commercial source were segregated into specific seed sizes and placed in storage conditions approximating commercial conditions to determine the amino acid changes taking place during storage within various size seeds. Concentrations of the isolated free amino acid fractions significantly decreased with seed size except for phenylalanine which significantly increased with seed size. Significant changes also occurred in the free amino acid fractions across storage periods up to nine months in duration. These results are the first to document a change in amino acids during the storage of peanuts.

scholarly journals Short-Term Stability of Biomarkers of Oxidative Stress and Antioxidant Status in Human Serum

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
Eugène H. J. M. Jansen ◽  
Piet K. Beekhof ◽  
Johannes W. J. M. Cremers ◽  
Dale Viezeliene ◽  
Vladimira Muzakova ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Human Serum ◽  
Antioxidant Status ◽  
Small Deviation ◽  
Storage Conditions ◽  
Short Term ◽  
Serum Samples ◽  
Antioxidant Assays ◽  
And Performance ◽  
Short Time

The oxidation and antioxidant status of serum are often determined in serum samples which have been frozen for some time. The oxidative stress process is prone to fast alterations in the sample because of the possible instability of the reactants. Here one oxidation assay (ROM) and three antioxidant assays (FRAP, TAS, and BAP) have been tested on their performance and stability at short-time storage. The most commonly used temperatures for storage and handling of serum samples (+4 and +20°C) were selected. In three short-term studies in which the storage time varied between 3 and 48 hrs the performance of these assays were tested on human serum samples. The general conclusion is that most assays performed well and gave stable results during 2 days of storage of the samples at both temperatures. Only the FRAP and TAS assays showed a small deviation at some storage conditions. In conclusion, handling of serum samples at +4 and +20°C during short-time periods did not affect the quality and performance of the oxidation and antioxidant assays during day-to-day analyses.

scholarly journals Establishment of a procedure to determine the content of 17 amino acids in soft-shell crab (Scylla sp.)

2020 ◽  
Vol 18 (3) ◽  
pp. 487-495
Author(s):  
Nguyen Phuong Lan ◽  
Do Thi Thanh Trung ◽  
Van Thu Vu ◽  
Le Tat Thanh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Content ◽  
Large Scale ◽  
Amino Acid Content ◽  
Dry Weight ◽  
Production Costs ◽  
Asia Pacific ◽  
Bioactive Substances ◽  
Soft Shell

Mud crab Scylla sp. is a common sea crab species in Vietnam as well as in Asia Pacific. Today, mud crabs are raised on a large scale to be harvested at the soft molting stage because of the high economic value of the finished shell crabs. At present, the processing of soft shell crabs is limited to whole packaging and exporting. However, 30% of soft-shelled crabs in processing often lose their feet and claws, which reduce production costs. Therefore, it is necessary to study the technology of processing soft-shell crabs to improve the value of soft-shelled crab products. Recently, the application of enzymes in processing has brought many benefits such as being environmentally friendly and creating many bioactive substances. In this journal, we built the procedure to determine amino acid content in the processing of Scylla sp. to ensure the quality of products obtained after processing. This procedure based on HPLC using a fluorescence reader. The results showed that the amino acid content after hydrolysis process by enzyme technology reached 65.58% dry weight and contains many valuable amino acids such as lysine, leucine, valine, methionine, histidine.

scholarly journals Coconut Carbon Dots: Progressive Large-Scale Synthesis, Detailed Biological Activities and Smart Sensing Aptitudes towards Tyrosine

Nanomaterials ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 162
Author(s):  
Pooja Chauhan ◽  
Deepa Mundekkad ◽  
Amitava Mukherjee ◽  
Savita Chaudhary ◽  
Ahmad Umar ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Carbon Dots ◽  
Large Scale ◽  
Limit Of Detection ◽  
Biological Activities ◽  
Biologically Active ◽  
Active Components ◽  
Ongoing Research ◽  
Amino Acid Sensing

In the recent era, carbon dots (C-dots) have been extensively considered as a potential tool in drug delivery analysis. However, there have been fewer reports in the literature on their application in the sensing of amino acids. As part of our ongoing research on coconut-husk-derived C-dots, we synthesized C-dots under different temperature conditions and utilized them in the field of amino acid sensing and found them to be highly selective and sensitive towards tyrosine. The detailed characterization of the prepared C-dots was carried out. The developed C-dots exhibit good values of quantum yield. BSA, HSA and glutamic acid were utilized to explore the binding efficiency of C-dots with biologically active components. Hemolysis, blood clotting index activity and cell viability assays using the prepared C-dots were evaluated and they were found to be biocompatible. Therefore, the C-dots described in this work have high potential to be utilized in the field of amino acid sensing, especially L-tyrosine. The limit of detection and the binding constant for the developed C-dots in the presence of tyrosine were found to be 0.96 nM and 296.38 nM−1, respectively. The efficiency of the developed C-dots was also investigated in the presence of various other amino acids and different water mediums in order to enhance the working scope of the developed sensors.

scholarly journals The genomic basis of electrotaxis in Dictyostelium discoideum: Electric field sensitive amino acids are dynamically encoded en masse for the streaming-stage proteome

2015 ◽  
Author(s):  
Albert J Erives
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Electric Field ◽  
Electric Fields ◽  
Large Scale ◽  
Genetic Model ◽  
Critical Role ◽  
Axon Growth ◽  
Amino Acid Residues ◽  
Signaling Systems

Electrotaxis plays a critical role in developmental cell migration, axon growth cone guidance, epithelial wound healing, tissue regeneration, and the degree of invasiveness characterizing different cancer cell lines. During electrotaxis in a direct current electric field (EF), a cell migrates preferentially either towards the anode or cathode depending on the cell-type. However, the types and ranges of mechanisms coupling trans-cellular electric fields to cellular EF-sensitive signaling systems are largely unknown. To address this cell biological phenomenon, I use transcriptomic data from a developmental genetic model in which multicellular social aggregation is induced by starvation of amoeboid cells. I find that the developmental proteome expressed during the streaming aggregation stage is measurably and substantially enriched in charged and highly polar amino acids relative to the proteomes of either the unicellular amoeboid or the multicellular fruiting body. This large-scale coding augmentation of EF-sensitive amino acid residues in thousands of streaming-specific proteins is accompanied by a proportional coding decrease in the number of small, uncharged amino acid residues. I also confirm an expected coding increase of biosynthetically costly amino acids in the proteome of the satiated feeding-stage amoeboid. These findings suggest that electrotactic capability is encoded broadly in the genetically regulated deployment of a developmental proteome with augmented EF-sensitivity. These results signify that extreme, nonuniform, evolutionary constraints can be exerted on the amino acid composition of an organism’s proteome.

Discrimination of cysteamine from mercapto amino acids through isoelectric point-mediated surface ligand exchange of β-cyclodextrin-modified gold nanoparticles

2020 ◽  
Vol 8 (18) ◽  
pp. 4039-4045
Author(s):  
Quanbao Ma ◽  
Xun Fang ◽  
Junting Zhang ◽  
Lili Zhu ◽  
Xiabing Rao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Gold Nanoparticles ◽  
Human Serum ◽  
Isoelectric Point ◽  
Ligand Exchange ◽  
Serum Samples ◽  
Human Serum Samples ◽  
Surface Ligand ◽  
First Time ◽  
Surface Ligand Exchange

A pI-mediated R6G-β-CD@AuNPs system was designed for the first time for the discrimination of CA from GSH/Cys/Hcy in human serum samples.

scholarly journals LC–MS/MS Analysis of Thiol-Containing Amino Acids in Exosomal Fraction of Serum

2020 ◽  
Vol 58 (7) ◽  
pp. 636-640
Author(s):  
Mayu Onozato ◽  
Kana Kobata ◽  
Tatsuya Sakamoto ◽  
Hideaki Ichiba ◽  
Takeshi Fukushima
Keyword(s):  
Oxidative Stress ◽  
Mass Spectrometry ◽  
Amino Acids ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Human Serum ◽  
Precolumn Derivatization ◽  
Tandem Mass ◽  
Chromatography Tandem Mass Spectrometry ◽  
Liquid Chromatography Tandem Mass

Abstract It has been suggested that thiol-containing amino acids could be used as biomarkers for diseases associated with oxidative stress. We investigated the thiol-containing amino acids, homocysteine (Hcy), cysteine (Cys), glutathione (GSH) and γ-glutamylcysteine (γ-GluCys), in commercial human serum by using liquid chromatography–tandem mass spectrometry (LC–MS/MS) after precolumn derivatization with 4-fluoro-7-sulfobenzofurazan. This method was applied to determine the composition of thiol-containing amino acids in exosomes prepared from the serum. Hcy, Cys, GSH and γ-GluCys could be detected in the exosomal fraction, and the ratio of each thiol-containing amino acid was similar to those in the corresponding native serum. Cys (94.76%) was most enriched in the exosomal fraction, followed by GSH (2.97%), γ-GluCys (1.59%) and Hcy (0.68%). These findings suggest that thiol-containing amino acids, Hcy, Cys, GSH and γ-GluCys, are included in exosomes in human serum.

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