Simple and reliable serotonin assay in human serum by LC-MS/MS method coupled with one step protein precipitation for clinical testing in patients with carcinoid tumors

2020 ◽  
Vol 1158 ◽  
pp. 122395
Author(s):  
Ying Shen ◽  
Xia Luo ◽  
Huijun Li ◽  
Zhongju Chen ◽  
Qing Guan ◽  
...  
2005 ◽  
Vol 49 (8) ◽  
pp. 3569-3571 ◽  
Author(s):  
GholamAli Khoschsorur ◽  
Franz Fruehwirth ◽  
Sieglinde Zelzer

ABSTRACT A simple, specific method is presented for simultaneous determination of voriconazole and itraconazole and its metabolite, hydroxyitraconazole, in human serum using one-step liquid-liquid extraction and high-performance liquid chromatography. Linearity tests ranged from 0.1 to 8.0 μg/ml; the minimum detectable concentration was 0.03 μg/ml.


Polymers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1017 ◽  
Author(s):  
Tatiana V. Plisko ◽  
Alexandr V. Bildyukevich ◽  
Katsiaryna S. Burts ◽  
Sergey S. Ermakov ◽  
Anastasia V. Penkova ◽  
...  

A novel method for one-step preparation of antifouling ultrafiltration membranes via a non-solvent induced phase separation (NIPS) technique is proposed. It involves using aqueous 0.05–0.3 wt.% solutions of cationic polyelectrolyte based on a copolymer of acrylamide and 2-acryloxyethyltrimethylammonium chloride (Praestol 859) as a coagulant in NIPS. A systematic study of the effect of the cationic polyelectrolyte addition to the coagulant on the structure, performance and antifouling stability of polysulfone membranes was carried out. The methods for membrane characterization involved scanning electron microscopy (SEM), atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FTIR), contact angle and zeta-potential measurements and evaluation of the permeability, rejection and antifouling performance in human serum albumin solution and surface water ultrafiltration. It was revealed that in the presence of cationic polyelectrolyte in the coagulation bath, its concentration has a major influence on the rate of “solvent–non-solvent” exchange and thus also on the rate of phase separation which significantly affects membrane structure. The immobilization of cationic polyelectrolyte macromolecules into the selective layer was confirmed by FTIR spectroscopy. It was revealed that polyelectrolyte macromolecules predominately immobilize on the surface of the selective layer and not on the bottom layer. Membrane modification was found to improve the hydrophilicity of the selective layer, to increase surface roughness and to change zeta-potential which yields the substantial improvement of membrane antifouling stability toward natural organic matter and human serum albumin.


INDIAN DRUGS ◽  
2019 ◽  
Vol 56 (07) ◽  
pp. 23-32
Author(s):  
P. C. Mehendale ◽  
R. B Athawale ◽  
K. K. Singh ◽  

A rapid and simple bio-analytical method with one step protein precipitation and extraction using acetonitrile as extraction solvent was developed for docetaxel. The extraction efficiency was 87.81% with satisfactory separation of docetaxel and IS peaks by isocratic elution with C18 column (25 cm X 4.5 mm, 0.5μm), acetonitrile and water (53:47 % V/V) as a mobile phase at ambient temperature and flow rate of 1mL/min. Paclitaxel solution in acetonitrile (10 mcg/ mL) was used as internal standard. The calibration curve was linear over the concentration range 50 – 5000 ng/mL, regression coefficient R2= 0.99936 and slope 0.00034. The limit of quantification and limit of detection were found to be 33 ng/ mL and 100 ng/mL, respectively. Coefficient of variation for within day and between the days was in the range of 10.9 to 14.9 and 12.5 to 15.05, respectively. Accuracy of the method indicated % recovery of 97.92 – 104.24%. Thus, a precise, accurate and robust method was developed and validated as per FDA guidelines.


1979 ◽  
Vol 181 (3) ◽  
pp. 779-781 ◽  
Author(s):  
D W Hutchinson ◽  
D S Mutopo

A one-step procedure has been developed for the preparation of [3H]bilirubin IX-alpha in good yield from unlabelled bilirubin. Irradiation of an aqueous solution of [3H]bilirubin IX-alpha in the presence of human serum albumin results in the covalent attachment of the bilirubin to the protein. Preliminary degradation studies have been carried out to locate the site of attachment of the bilirubin to the albumin.


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