scholarly journals Dihydrofolate reductase: low-resolution mass-spectrometric analysis of an elastase digest as a sequencing tool

1974 ◽  
Vol 137 (2) ◽  
pp. 409-411 ◽  
Author(s):  
Howard R. Morris ◽  
Karen E. Batley ◽  
Nigel G. L. Harding ◽  
Richard A. Bjur ◽  
John G. Dann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Dihydrofolate Reductase ◽  
Mass Spectrometric ◽  
Spectrometric Analysis ◽  
Small Peptides ◽  
Molecular Weight Range ◽  
Unknown Structure ◽  
Resolution Mass ◽  
The Ideal

An elastase digest of a protein of unknown structure, dihydrofolate reductase, was studied by mass spectrometry. This soluble digest contained a large number of small peptides in different yields, within the ideal molecular-weight range (200–1200) for mixture-analysis mass spectrometry. Sequences of the major component peptides in the digest are reported.

MO430MASS-SPECTROMETRIC IDENTIFICATION OF POST-TRANSLATIONAL GUANIDINYLATED PROTEINS IN THE CONTEXT OF SYSTEMIC LUPUS ERYTHEMATOSUS

2021 ◽  
Vol 36 (Supplement_1) ◽  
Author(s):  
Juliane Hermann ◽  
Ute Raffetseder ◽  
Michaela Lellig ◽  
Joachim Jankowski ◽  
Vera Jankowski
Keyword(s):  
Mass Spectrometry ◽  
Systemic Lupus Erythematosus ◽  
High Resolution ◽  
Lupus Erythematosus ◽  
Imaging Techniques ◽  
Mass Spectrometric ◽  
Mass Spectrometric Imaging ◽  
Systemic Lupus ◽  
Notch 3 ◽  
Resolution Mass

Abstract Background and Aims With continuous identification of post-translational modified isoforms of proteins, it is becoming increasingly clear that post-translational modifications limit or modify the biological functions of native proteins are majorly involved in development of various chronic disease. This is mostly due to technically advanced molecular identification and quantification methods, mainly based on mass spectrometry. Mass spectrometry has become one of the most powerful tools for the identification of lipids. Method In this study, we used sophisticated high-resolution mass-spectrometric methods to analyze the soluble ligand of receptor Notch-3, namely the Y-box protein (YB)-1, in serum from systemic lupus erythematosus (SLE) patients. In addition, kidneys of lupus-prone (MRL.lpr) mice were analyzed by mass-spectrometric imaging techniques to identify the underlying pathomechanisms. Serum YB-1 was isolated by chromatographic methods, afterwards digested by trypsin and analyzed by matrix assisted laser desorption/ionization mass spectrometry (MALDI-MS). The kidneys were fixed in paraffin, then kidney sections were deparaffinized, tryptic digested and analyzed by mass-spectrometric imaging techniques. Mass-spectrometry of extracellular YB-1 in SLE patient serum revealed post-translational guanidinylation of two lysine’s within the highly conserved cold shock domain (CSD) of the YB-1 protein (YB-1-2G). Patients with increased disease activity and those with active renal involvement (lupus nephritis, LN) had a higher degree of dual-guanidinylation within the CSD. Of note, at least one of these modifications was present in all analyzed LN patients, whereas single-guanidinylated YB-1 was present in only one and double modification in none of the control individuals. Mass-spectrometric imaging analyses specifically localized YB-1-2G and increases Notch-3 expression in kidney sections from MRL.lpr mice. Results The data from this study clearly demonstrate the high potential of high-resolution mass spectrometric methods as well as mass spectrometric imaging techniques to identify pathomechanisms of diseases like SLE/LN.

Direct analysis of herbicides by paper spray ionization mass spectrometry

2015 ◽  
Vol 7 (23) ◽  
pp. 9808-9816 ◽  
Author(s):  
Steven L. Reeber ◽  
Sneha Gadi ◽  
Sung-Ben Huang ◽  
Gary L. Glish
Keyword(s):  
Mass Spectrometry ◽  
Environmental Samples ◽  
Direct Analysis ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Ionization Mass ◽  
Paper Spray ◽  
Paper Spray Ionization ◽  
Rapid Mass

Paper spray ionization enables the rapid mass spectrometric analysis of environmental samples without the use of chromatography or sample cleanup techniques.

scholarly journals Mass Spectrometric Analysis of Multiple Pertussis Toxins and Toxoids

2010 ◽  
Vol 2010 ◽  
pp. 1-9 ◽  
Author(s):  
Yulanda M. Williamson ◽  
Hercules Moura ◽  
David Schieltz ◽  
Jon Rees ◽  
Adrian R. Woolfitt ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Immune Response ◽  
Mass Spectrometric ◽  
Peptide Sequence ◽  
Spectrometric Analysis ◽  
Vaccine Preventable Disease ◽  
Label Free ◽  
Chemically Modified ◽  
Quantification Method ◽  
Major Virulence Factor

Bordetella pertussis(Bp) is the causative agent of pertussis, a vaccine preventable disease occurring primarily in children. In recent years, there has been increased reporting of pertussis. Current pertussis vaccines are acellular and consist of Bp proteins including the major virulence factor pertussis toxin (Ptx), a 5-subunit exotoxin. Variation in Ptx subunit amino acid (AA) sequence could possibly affect the immune response. A blind comparative mass spectrometric (MS) analysis of commercially available Ptx as well as the chemically modified toxoid (Ptxd) from licensed vaccines was performed to assess peptide sequence and AA coverage variability as well as relative amounts of Ptx subunits. Qualitatively, there are similarities among the various sources based on AA percent coverages and MS/MS fragmentation profiles. Additionally, based on a label-free mass spectrometry-based quantification method there is differential relative abundance of the subunits among the sources.

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