Automated protein identification using MALDI mass spectrometry

2000 ◽  
Vol 28 (5) ◽  
pp. A260-A260
Author(s):  
D. Gostick ◽  
J. Brown ◽  
A. Dobbins ◽  
E. Kapp ◽  
R. O'malley ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Identification ◽  
Maldi Mass Spectrometry

scholarly journals Peptide and protein analysis with mass spectrometry

2002 ◽  
Vol 16 (1) ◽  
pp. 15-28 ◽  
Author(s):  
Sunia A. Trauger ◽  
William Webb ◽  
Gary Siuzdak
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Protein Identification ◽  
Data Interpretation ◽  
Maldi Mass Spectrometry ◽  
Protein Characterization ◽  
Accurate Information ◽  
Molecular Weight Determination ◽  
Peptide Fragments ◽  
Identification And Characterization

Mass spectrometry (MS) is rapidly becoming a fundamental tool for biologists and biochemists in their efforts to characterize cellular function. Recent advancements in MS technology and front-end methodologies, along with the completion of the human genome have greatly popularized its use by researchers for protein identification and characterization. This paper is a general overview of how mass spectrometry is being used for the analysis of peptides and proteins, focusing on its application to molecular weight determination. Sample preparatory and cleanup techniques used in our laboratory for protein and peptide analysis are provided, along with a discussion of data interpretation. The utility of mass spectrometry for protein and peptide analyses lies in its ability to provide highly accurate molecular weight information on intact molecules. The ability to generate such accurate information can be extremely useful for protein identification and characterization. For example, a protein can often be unambiguously identified by the accurate mass analysis of its constituent peptides produced by either chemical or enzymatic treatment of the sample. Furthermore, protein identification can also be facilitated by analysis of the protein's proteolytic peptide fragments in the gas phase; fragment ions generated inside the mass spectrometer via collision-induced dissociation (CID) to yield information about the primary structure and modifications. This overview describes how electrospray ionization (ESI) and matrix‒assisted laser desorption/ionization (MALDI) mass spectrometry is being used for peptide and protein characterization focusing on its application to molecular weight determination.

Time-dependent cortisol turnover in tissues using stable isotope tracers and MALDI Mass Spectrometry (MS) sampling

2018 ◽  
Author(s):  
Shazia Khan ◽  
Diego F Cobice ◽  
Dawn EW Livingstone ◽  
C Logan Mackay ◽  
Scott P Webster ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Maldi Mass Spectrometry ◽  
Time Dependent ◽  
Stable Isotope Tracers ◽  
Isotope Tracers

Mass Spectrometry Techniques: Principles and Practices for Quantitative Proteomics

2020 ◽  
Vol 21 ◽  
Author(s):  
Rocco J. Rotello ◽  
Timothy D. Veenstra
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Proteomics ◽  
Protein Identification ◽  
Dynamic Nature ◽  
Complete Coverage ◽  
The Past ◽  
Proteome Level ◽  
A Cell ◽  
Quantitative Changes ◽  
Made In

: In the current omics-age of research, major developments have been made in technologies that attempt to survey the entire repertoire of genes, transcripts, proteins, and metabolites present within a cell. While genomics has led to a dramatic increase in our understanding of such things as disease morphology and how organisms respond to medications, it is critical to obtain information at the proteome level since proteins carry out most of the functions within the cell. The primary tool for obtaining proteome-wide information on proteins within the cell is mass spectrometry (MS). While it has historically been associated with the protein identification, developments over the past couple of decades have made MS a robust technology for protein quantitation as well. Identifying quantitative changes in proteomes is complicated by its dynamic nature and the inability of any technique to guarantee complete coverage of every protein within a proteome sample. Fortunately, the combined development of sample preparation and MS methods have made it capable to quantitatively compare many thousands of proteins obtained from cells and organisms.

Application of Carbon Matrices to Screening Pentacylic Triterpenoids in Plant Feedstock by MALDI Mass Spectrometry

2020 ◽  
Vol 75 (14) ◽  
pp. 1749-1757
Author(s):  
E. A. Anikeenko ◽  
E. N. Rakhmatullina ◽  
D. I. Falev ◽  
O. Yu. Khoroshev ◽  
N. V. Ul’yanovskii ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Maldi Mass Spectrometry ◽  
Plant Feedstock

scholarly journals Sample preparation strategy for the detection of steroid-like compounds using MALDI mass spectrometry imaging: pulmonary distribution of budesonide as a case study

2021 ◽  
Author(s):  
Riccardo Zecchi ◽  
Pietro Franceschi ◽  
Laura Tigli ◽  
Davide Amidani ◽  
Chiara Catozzi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Mass Spectrometry Imaging ◽  
Maldi Mass Spectrometry ◽  
Adult Rabbit ◽  
Chronic Obstructive ◽  
Ionization Mass ◽  
Obstructive Pulmonary Disease ◽  
Imaging Protocol ◽  
Girard’S Reagent

AbstractCorticosteroids as budesonide can be effective in reducing topic inflammation processes in different organs. Therapeutic use of budesonide in respiratory diseases, like asthma, chronic obstructive pulmonary disease, and allergic rhinitis is well known. However, the pulmonary distribution of budesonide is not well understood, mainly due to the difficulties in tracing the molecule in lung samples without the addition of a label. In this paper, we present a matrix-assisted laser desorption/ionization mass spectrometry imaging protocol that can be used to visualize the pulmonary distribution of budesonide administered to a surfactant-depleted adult rabbit. Considering that budesonide is not easily ionized by MALDI, we developed an on-tissue derivatization method with Girard’s reagent P followed by ferulic acid deposition as MALDI matrix. Interestingly, this sample preparation protocol results as a very effective strategy to raise the sensitivity towards not only budesonide but also other corticosteroids, allowing us to track its distribution and quantify the drug inside lung samples. Graphical abstract

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