scholarly journals Optimization of a minimal sample preparation protocol for imaging mass spectrometry of unsectioned juvenile invertebrates

2019 ◽  
Vol 55 (4) ◽  
pp. e4458 ◽  
Author(s):  
Katherine E. Zink ◽  
Denise A. Tarnowski ◽  
Mark J. Mandel ◽  
Laura M. Sanchez
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Imaging Mass Spectrometry ◽  
Minimal Sample

scholarly journals Trypsin and MALDI matrix pre-coated targets simplify sample preparation for mapping proteomic distributions within biological tissues by imaging mass spectrometry

2016 ◽  
Vol 51 (12) ◽  
pp. 1168-1179 ◽  
Author(s):  
Faizan Zubair ◽  
Paul E. Laibinis ◽  
William G. Swisher ◽  
Junhai Yang ◽  
Jeffrey M. Spraggins ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Imaging Mass Spectrometry ◽  
Biological Tissues ◽  
Maldi Matrix

scholarly journals Sample Preparation and Analysis for Imaging Mass Spectrometry

2017 ◽  
pp. 43-50 ◽  
Author(s):  
Genea Edwards ◽  
Annia Mesa ◽  
Robert I. Vazquez-Padron ◽  
Jane-Marie Kowalski ◽  
Sanjoy K. Bhattacharya
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Imaging Mass Spectrometry

scholarly journals High throughput screening of complex biological samples with mass spectrometry – from bulk measurements to single cell analysis

The Analyst ◽  
2019 ◽  
Vol 144 (3) ◽  
pp. 872-891 ◽  
Author(s):  
Emily E. Kempa ◽  
Katherine A. Hollywood ◽  
Clive A. Smith ◽  
Perdita E. Barran
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
High Throughput ◽  
High Throughput Screening ◽  
Single Cell Analysis ◽  
State Of The Art ◽  
Cell Analysis ◽  
Biotechnological Applications ◽  
Biological Matrices ◽  
Minimal Sample

We review the state of the art in HTS using mass spectrometry with minimal sample preparation from complex biological matrices. We focus on industrial and biotechnological applications.

Comparing ELISA and LC-MS/MS: A Simple, Targeted Postmortem Blood Screen

2021 ◽  
Author(s):  
Dina M Swanson ◽  
Julia M Pearson ◽  
Theresa Evans-Nguyen
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Limit Of Detection ◽  
Screening Method ◽  
Chemical Properties ◽  
Forensic Toxicology ◽  
Enzyme Linked Immunosorbent Assay ◽  
Minimal Sample ◽  
Elisa Testing ◽  
Postmortem Blood

Abstract A comprehensive screening method that is specific, accurate, and customizable is necessary in any forensic toxicology laboratory. Most laboratories utilize some form of immunoassay testing as it is reliable and sensitive with minimal sample preparation and is relatively inexpensive to simultaneously screen for multiple classes of drugs with different chemical properties. However, accessibility to more specific technology and instrumentation such as mass spectrometry has increased and therefore using immunoassay as the screening method of choice may be revisited. A screening method for 42 drugs in postmortem blood was developed and validated following the Organization of Scientific Area Committees for Forensic Science (OSAC) guidelines for toxicology method validation. The method was developed using minimal sample preparation of postmortem blood consisting only of a protein precipitation. Only two internal standards were used which greatly reduces the cost of implementing this method. Limit of detection (LOD), interference studies, processed sample stability and ion suppression/enhancement were examined. Additionally, over 100 case samples were analyzed by both the current enzyme linked immunosorbent assay (ELISA) testing procedure and the proposed liquid chromatography tandem mass spectrometry (LC-MS/MS) screening method. The comparison determined that the LC/MS-MS method performed as well as or better than the ELISA in nearly all cases. The ability to add additional target drugs increases the laboratory’s scope of analysis as well. This method is ideal for forensic laboratories wishing to improve screening while working within budget constraints.

Spatial Metabolomics of the Human Kidney Using MALDI Trapped Ion Mobility Imaging Mass Spectrometry

2020 ◽  
Author(s):  
Elizabeth Neumann ◽  
Lukasz Migas ◽  
Jamie L. Allen ◽  
Richard Caprioli ◽  
Raf Van de Plas ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Imaging Mass Spectrometry ◽  
Structural Complexity ◽  
Human Kidney ◽  
Resolving Power ◽  
Mobility Separation ◽  
Trapped Ion ◽  
Mobility Data ◽  
Ion Mobility Separation

<div> <div> <p>Small metabolites are essential for normal and diseased biological function but are difficult to study because of their inherent structural complexity. MALDI imaging mass spectrometry (IMS) of small metabolites is particularly challenging as MALDI matrix clusters are often isobaric with metabolite ions, requiring high resolving power instrumentation or derivatization to circumvent this issue. An alternative to this is to perform ion mobility separation before ion detection, enabling the visualization of metabolites without the interference of matrix ions. Here, we use MALDI timsTOF IMS to image small metabolites at high spatial resolution within the human kidney. Through this, we have found metabolites, such as arginic acid, acetylcarnitine, and choline that localize to the cortex, medulla, and renal pelvis, respectively. We have also demonstrated that trapped ion mobility spectrometry (TIMS) can resolve matrix peaks from metabolite signal and separate both isobaric and isomeric metabolites with different localizations within the kidney. The added ion mobility data dimension dramatically increased the peak capacity for molecular imaging experiments. Future work will involve further exploring the small metabolite profiles of human kidneys as a function of age, gender, and ethnicity.</p></div></div>

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