A Novel Combined Microstrip Resonator/Nanospray Ionization Source for Microwave-Assisted Trypsin Digestion of Proteins

2020 ◽  
Vol 31 (8) ◽  
pp. 1684-1696
Author(s):  
Maria E. Rivera-Albarran ◽  
Steven J. Ray
2000 ◽  
Vol 6 (2) ◽  
pp. 205-211 ◽  
Author(s):  
Danielle Promé ◽  
Jean-Claude Promé ◽  
Henri Wajcman ◽  
Jean Riou ◽  
Frédéric Galactéros ◽  
...  

Hemoglobin (Hb) Neuilly-sur-Marne is a new α-chain variant found during a systematic screening. Electrospray mass measurements showed the presence of an abnormal α-chain displaying a shift of +315 u relative to the normal value. Tryptic cleavage of this chain and molecular weight determination of the peptides indicated that the 315 u shift was located into the αT-9 peptide, the molecular weight of which is higher than 3000 Da. High-energy collision spectra of MH+ ions generated by liquid secondary ion mass spectrometry from the normal and abnormal αT-9 afforded mainly amino-terminal containing ions. They indicated that these two peptides have an identical amino acid sequence from their 1st to 25th residues, the mass increase being thus located beyond this point. Too few ions were formed to establish reliably the sequence forward. It was hypothesized that this mass shift could result from a repeated sequence since the sum of the mass of the three residues—leucine, serine and aspartic acid—preceding position 25 is exactly 315 u. To get sequence information above position 25, decomposition of multicharged species was attempted. An ion trap fitted with a nanospray ionization source was used. It produced mainly triply- and quadruply-charged ions. Decomposition of the triply-charged ion afforded a series of singly-charged Y-ions in the expected region, giving a readily interpretable sequence. It confirmed the insertion of a Ser-Asp-Leu sequence above position 25. Surprisingly, decomposition of the quadruply-charged molecular ion gave too few ions to provide sequence information in the expected region. Spectra were dominated by some multicharged Y ions arising from cleavages close to the amino end. Tandem mass spectrometry experiments were performed on the abundant Y303+ ion and produced again a singly-charged Y ion series in the suitable domain which confirmed the above result. In Hb Neuilly-sur Marne this insertion of the Ser-Asp-Leu residues. between positions α-86 and α-87 is very likely due to a slipped strand mispairing mechanism.


2007 ◽  
Vol 6 (1) ◽  
pp. 263-272 ◽  
Author(s):  
Nan Wang ◽  
Lauren MacKenzie ◽  
Andrea G. De Souza ◽  
Hongying Zhong ◽  
Greg Goss ◽  
...  

2007 ◽  
Vol 17 (8) ◽  
pp. 1567-1574 ◽  
Author(s):  
R R A Syms ◽  
H Zou ◽  
M Bardwell ◽  
M-A Schwab

2021 ◽  
Vol 17 (1) ◽  
Author(s):  
Ana Cláudia Raposo ◽  
Carlito Lebrilla ◽  
Ricardo Wagner Portela ◽  
Gege Xu ◽  
Arianne Pontes Oriá

Abstract Background Glycoproteins are important tear components that participate in the stability of the ocular surface. However, the glycopeptides that are present in the tears of wild animals have not yet been described. This work aimed to describe the glycoproteomic profile of roadside hawk (Rupornis magnirostris) and caiman (Caiman latirostris) tears. Methods Tears collected from 10 hawks and 70 caimans using Schirmer tear test strips were used in this study. The samples were submitted to trypsin digestion and separated using a reverse-phase column coupled to a mass spectrometer associated to a nanospray ionization source. The glycoproteins were categorized as: cellular components, biological processes and molecular function, according to the UniProt Knowledgebase. Results As shown by the liquid chromatography–mass spectrometry, all glycopeptides found were classified as N-type. Of the 51 glycoproteins that were identified in the hawk tear film, the most abundant were ovotransferrin, globulins and complement system proteins. In the caiman tear film, 29 glycoproteins were identified. The most abundant caiman glycoproteins were uncharacterized proteins, ATPases, globulins and proteasome components. Ontological characterization revealed that the glycoproteins were extracellular, and the most identified molecular function was endopeptidase activity for both species. Conclusion Glycoproteins are abundant in the tear film of the bird and reptile species studied herein, and all these molecules were shown to have N-type modifications. Location at the extracellular space and an endopeptidase inhibitor activity were the main cell component and molecular function for both species, respectively. These profiles showed differences when compared to human tears, are possibly linked to adaptive processes and can be the basis for further studies on the search of disease biomarkers.


Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
I Stanisavljević ◽  
M Lazić ◽  
N Radulović ◽  
V Veljković

2015 ◽  
Author(s):  
Corinne Fruit ◽  
Julien Godeau ◽  
Marine Harari ◽  
Sylvain Laclef ◽  
Vincent Levacher ◽  
...  

Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak

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