Capillary electrophoretic and micellar electrokinetic separations of asymmetric dimethyl-L-arginine and structurally related amino acids: Quantitation in human plasma

2004 ◽  
Vol 27 (17-18) ◽  
pp. 1483-1490 ◽  
Author(s):  
Gabriele Trapp ◽  
Karsten Sydow ◽  
Maria T. Dulay ◽  
Tina Chou ◽  
John P. Cooke ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Plasma ◽  
Electrokinetic Separations ◽  
Capillary Electrophoretic

scholarly journals Determination of Branched-Chain Amino Acids in Food Supplements and Human Plasma by a CE-MS/MS Method with Enhanced Resolution

2021 ◽  
Vol 22 (15) ◽  
pp. 8261
Author(s):  
Juraj Piestansky ◽  
Michaela Matuskova ◽  
Ivana Cizmarova ◽  
Dominika Olesova ◽  
Peter Mikus
Keyword(s):  
Amino Acids ◽  
Human Plasma ◽  
Limit Of Detection ◽  
Background Electrolyte ◽  
Branched Chain Amino Acids ◽  
Fused Silica ◽  
Suitable Alternative ◽  
Enhanced Resolution ◽  
Validation Parameters ◽  
Branched Chain

In the presented study, a capillary electrophoresis-mass spectrometry method combining high separation efficiency and sensitive detection has been developed and validated, for the first time, to quantify branched chain amino acids (valine, isoleucine, leucine) in commercial food and sport supplement samples and human plasma samples. The separations were performed in a bare fused silica capillary. The background electrolyte was composed of 500 mM formic acid with pH 2.0. The plasma sample pretreatment was realized by simple protein precipitation with acetonitrile. Injection of a short zone of highly basic electrolyte before the sample injection and application of the negative pressure on the separation were accompanied by enhanced resolution of the isobaric amino acids—isoleucine and leucine. The developed method was characterized by favorable validation parameters, such as linearity (r2 > 0.99), accuracy and precision, the limit of detection, lower limit of quantification, or robustness. These parameters were more than sufficient for the quantification of branched chain amino acids in various samples. The determined concentrations of branched chain amino acids in food and sports supplements were in very good agreement with the content declared by the manufacturer. The investigated concentrations of branched chain amino acids were in the range 294.68–359.24 µM for valine, 91.76–95.67 µM for isoleucine, and 196.78–251.24 µM for leucine. These concentrations fall within the physiological limits. The developed CE-MS/MS method represents a suitable alternative to traditional approaches used in branched chain amino acid quality control and bioanalysis.

Antibody to antihemophilic factor and its lack of reaction with hemophilic plasma

1965 ◽  
Vol 208 (3) ◽  
pp. 499-507 ◽  
Author(s):  
William D. McLester ◽  
Robert H. Wagner
Keyword(s):  
Amino Acids ◽  
Human Plasma ◽  
Measurable Effect ◽  
Rabbit Plasma ◽  
Canine Plasma ◽  
Inhibitor Titer ◽  
Antihemophilic Factor ◽  
Immune Rabbit

A partially purified preparation of canine antihemophilic factor was obtained utilizing amino acids as precipitating agents. This AHF preparation was used as the antigen in an immunologic investigation of canine hemophilia. Plasma from rabbits immunized with this preparation contained antibodies which inhibited the coagulation of normal canine plasma. The immune rabbit plasma inhibited AHF activity but had no measurable effect on any other procoagulant. Neither canine hemophilic plasma nor fractions prepared from canine hemophilic plasma contained an antigen capable of neutralizing the inhibitor (no cross-reacting material). The inhibitor titer was inversely proportional to the amount of added AHF in the form of a fraction of normal canine plasma. The inhibitor cross-reacted with human plasma AHF, but not with porcine, bovine, or rabbit AHF. The results of these studies are interpreted as providing further evidence that hemophilia, specifically canine hemophilia, is due to the failure of production of the antihemophilic factor.

scholarly journals Monitoring of Irinotecan in Human Plasma: Sensitive Fluorescent Nanogels by Molecular Imprinting

2019 ◽  
Author(s):  
Martina Tommasini ◽  
Elena Pellizzoni ◽  
Valentina Iacuzzi ◽  
Elena Marangon ◽  
Paola Posocco ◽  
...  
Keyword(s):  
Amino Acids ◽  
Fluorescence Quenching ◽  
Human Plasma ◽  
Molecular Imprinting ◽  
Plasma Sample ◽  
Direct Detection ◽  
Fluorescent Nanoparticles ◽  
High Dilution ◽  
Molecularly Imprinted

A series of fluorescent molecularly imprinted nanogels to detect irinotecan (CPT11) were prepared and characterized. A set of amino acids and napthalimide polymerisable derivatives allowed to obtain polymers as soluble fluorescent nanoparticles by high dilution imprinted synthesis. The direct detection of irinotecan in human plasma was obtained by fluorescence quenching of the naphtalimide-based imprinted materials. The plasma sample treated with acetonitrile allowed the detection of irinotecan in the 10nM – 30μM range. The LOD was 9.4 nM, with within-run variability 10% and day to day variability 13%.<br>

scholarly journals Development, validation and application of LC–MS/MS method for quantification of amino acids, kynurenine and serotonin in human plasma

2020 ◽  
Vol 180 ◽  
pp. 113018 ◽  
Author(s):  
Dávid Virág ◽  
Márton Király ◽  
László Drahos ◽  
Andrea Edit Édes ◽  
Kinga Gecse ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Plasma

Effect of Food Intake on Amino Acids in Human Plasma

1956 ◽  
Vol 4 (3) ◽  
pp. 275-278 ◽  
Author(s):  
E. STATEN WYNNE ◽  
CORA L. COTT
Keyword(s):  
Amino Acids ◽  
Food Intake ◽  
Human Plasma ◽  
Effect Of Food

Characterization of antithrombin III from human plasma by two-dimensional gel electrophoresis and capillary electrophoretic methods

2003 ◽  
Vol 24 (24) ◽  
pp. 4282-4290 ◽  
Author(s):  
Leopold Kremser ◽  
Andrea Brückner ◽  
Andrea Heger ◽  
Tom Grunert ◽  
Andrea Buchacher ◽  
...  
Keyword(s):  
Human Plasma ◽  
Gel Electrophoresis ◽  
Antithrombin Iii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Capillary Electrophoretic
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