Human Bone Paleoproteomics Utilizing the Single-Pot, Solid-Phase-Enhanced Sample Preparation Method to Maximize Detected Proteins and Reduce Humics

2018 ◽  
Vol 17 (11) ◽  
pp. 3976-3983 ◽  
Author(s):  
Timothy P. Cleland
Keyword(s):  
Sample Preparation ◽  
Preparation Method ◽  
Solid Phase ◽  
Human Bone ◽  
Sample Preparation Method

scholarly journals Micro Salting-Out Assisted Matrix Solid-Phase Dispersion: A Simple and Fast Sample Preparation Method for the Analysis of Bisphenol Contaminants in Bee Pollen

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2350
Author(s):  
Jianing Zhang ◽  
Fengjie Yu ◽  
Yunmin Tao ◽  
Chunping Du ◽  
Wenchao Yang ◽  
...  
Keyword(s):  
Sample Preparation ◽  
Preparation Method ◽  
Solid Phase ◽  
Sample Preparation Method ◽  
Salting Out ◽  
Bee Pollen ◽  
Matrix Solid Phase Dispersion ◽  
Phase Dispersion ◽  
New Strategy ◽  
Semi Solid

In the present work, a novel sample preparation method, micro salting-out assisted matrix solid-phase dispersion (μ-SOA-MSPD), was developed for the determination of bisphenol A (BPA) and bisphenol B (BPB) contaminants in bee pollen. The proposed method was designed to combine two classical sample preparation methodologies, matrix solid-phase dispersion (MSPD) and homogenous liquid-liquid extraction (HLLE), to simplify and speed-up the preparation process. Parameters of μ-SOA-MSPD were systematically investigated, and results indicated the significant effect of salt and ACN-H2O extractant on the signal response of analytes. In addition, excellent clean-up ability in removing matrix components was observed when primary secondary amine (PSA) sorbent was introduced into the blending operation. The developed method was fully validated, and the limits of detection for BPA and BPB were 20 μg/kg and 30 μg/kg, respectively. Average recoveries and precisions were ranged from 83.03% to 94.64% and 1.76% to 5.45%, respectively. This is the first report on the analysis of bisphenol contaminants in bee pollen sample, and also on the combination of MSPD and HLLE. The present method might provide a new strategy for simple and fast sample preparation of solid and semi-solid samples.

Alternative sample preparation method for photochemical studies based on solid phase microextraction: Synthetic pyrethroid photochemistry

2007 ◽  
Vol 1152 (1-2) ◽  
pp. 156-167 ◽  
Author(s):  
M. Fernández-Álvarez ◽  
L. Sánchez-Prado ◽  
M. Lores ◽  
M. Llompart ◽  
C. García-Jares ◽  
...  
Keyword(s):  
Sample Preparation ◽  
Solid Phase Microextraction ◽  
Preparation Method ◽  
Solid Phase ◽  
Synthetic Pyrethroid ◽  
Sample Preparation Method

scholarly journals Implementing solid-phase-enhanced sample preparation for Co-Immunoprecipitation with Mass Spectrometry for C. elegans

2021 ◽  
Author(s):  
Guelkiz Baytek ◽  
Oliver Popp ◽  
Philipp Mertins ◽  
Baris Tursun
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Protein Interactions ◽  
Molecular Mechanisms ◽  
Preparation Method ◽  
Solid Phase ◽  
Protein Protein Interactions ◽  
Sample Preparation Method ◽  
C Elegans

Studying protein-protein interactions in vivo can reveal key molecular mechanisms of biological processes. Co-Immunoprecipitation followed by Mass Spectrometry (CoIP-MS) allows detection of protein-protein interactions in high-throughput. The nematode Caenorhabditis elegans (C. elegans) is a powerful genetic model organism for in vivo studies. Yet, its rigid cuticle and complex tissues require optimization for protein biochemistry applications to ensure robustness and reproducibility of experimental outcomes. Therefore, we optimized CoIP-MS application to C. elegans protein lysates by combining a native CoIP procedure with an efficient sample preparation method called single-pot, solid-phase-enhanced, sample preparation method (SP3). Our results based on the subunits of the conserved chromatin remodeler FACT demonstrate that our SP3-integrated CoIP-MS procedure for C. elegans samples is highly accurate and robust. Moreover, in a previous study (Baytek et al. 2021), we extended our technique to studying the chromodomain factor MRG-1 (MRG15 in human), which resulted in unprecedented findings.

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