Identification of lanthionine and lysinoalanine in heat-treated wheat gliadin and bovine serum albumin using tandem mass spectrometry with higher-energy collisional dissociation

Amino Acids ◽  
2015 ◽  
Vol 48 (4) ◽  
pp. 959-971 ◽  
Author(s):  
Ine Rombouts ◽  
Marlies A. Lambrecht ◽  
Sebastien C. Carpentier ◽  
Jan A. Delcour
Keyword(s):  
Mass Spectrometry ◽  
Bovine Serum Albumin ◽  
Tandem Mass Spectrometry ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tandem Mass ◽  
Heat Treated ◽  
Wheat Gliadin

scholarly journals Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Ine Rombouts ◽  
Bert Lagrain ◽  
Katharina A. Scherf ◽  
Marlies A. Lambrecht ◽  
Peter Koehler ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electron Transfer ◽  
Bovine Serum Albumin ◽  
Tandem Mass Spectrometry ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Electron Transfer Dissociation ◽  
Tandem Mass ◽  
The Impact

Abstract Thermolysin hydrolyzates of freshly isolated, extensively stored (6 years, 6 °C, dry) and heated (60 min, 90 °C, in excess water) bovine serum albumin (BSA) samples were analyzed with liquid chromatography (LC) electrospray ionization (ESI) tandem mass spectrometry (MS/MS) using alternating electron-transfer dissociation (ETD) and collision-induced dissociation (CID). The positions of disulfide bonds and free thiol groups in the different samples were compared to those deduced from the crystal structure of native BSA. Results revealed non-enzymatic posttranslational modifications of cysteine during isolation, extensive dry storage and heating. Heat-induced extractability loss of BSA was linked to the impact of protein unfolding on the involvement of specific cysteine residues in intermolecular and intramolecular thiol-disulfide interchange and thiol oxidation reactions. The here developed approach holds promise for exploring disulfide bond formation and reshuffling in various proteins under conditions relevant for chemical, biochemical, pharmaceutical and food processing.

Interaction of Bovine Serum Albumin and Lysozyme with Stainless Steel Studied by Time-of-Flight Secondary Ion Mass Spectrometry and X-ray Photoelectron Spectroscopy

Langmuir ◽  
2012 ◽  
Vol 28 (47) ◽  
pp. 16306-16317 ◽  
Author(s):  
Yolanda S. Hedberg ◽  
Manuela S. Killian ◽  
Eva Blomberg ◽  
Sannakaisa Virtanen ◽  
Patrik Schmuki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stainless Steel ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Secondary Ion Mass Spectrometry ◽  
Time Of Flight ◽  
X Ray ◽  
Secondary Ion

Gel formation in heat-treated bovine serum albumin–κ-carrageenan systems

2000 ◽  
Vol 14 (2) ◽  
pp. 95-110 ◽  
Author(s):  
S Neiser ◽  
K.I Draget ◽  
O Smidsrød
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gel Formation ◽  
Heat Treated

scholarly journals Interactions between Orange II and Components in Heat-Treated Bovine Serum Albumin

1982 ◽  
Vol 31 (12) ◽  
pp. 988-992
Author(s):  
Koichiro AOKI ◽  
Koji ONDA ◽  
Shuji OKUMURA ◽  
Mamoru MURATA ◽  
Koichi HIRAMATSU
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Orange Ii ◽  
Heat Treated

scholarly journals Identifying Reducing and Capping Sites of Protein-Encapsulated Gold Nanoclusters

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1630 ◽  
Author(s):  
Yu-Chen Hsu ◽  
Mei-Jou Hung ◽  
Yi-An Chen ◽  
Tsu-Fan Wang ◽  
Ying-Ru Ou ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Local Structure ◽  
Bovine Serum ◽  
Gold Nanoclusters ◽  
Cysteic Acid ◽  
Subsequent Growth ◽  
The Core

The reducing and capping sites along with their local structure impact photo properties of the red bovine serum albumin-capped Au nanocluster (BSA-AuNC), however, they are hard to identify. We developped a workflow and relevant techniques using mass spectrometry (MS) to identify the reducing and capping sites of BSA-AuNCs involved in their formation and fluorescence. Digestion without disulfide cleavages yielded an Au core fraction exhibiting red fluorescence and [AunSm] ion signals and a non-core fraction exhibiting neither of them. The core fraction was identified to mainly be comprised of peptides containing cysteine residues. The fluorescence and [AunSm] signals were quenched by tris(2-carboxyethyl)phosphine, confirming that disulfide groups were required for nanocluster stabilization and fluorescence. By MS sequencing, the disulfide pairs, C75–C91/C90–C101 in domain IA, C315–C360/C359–C368 in domain IIB, and C513–C558/C557–C566 in domain IIIB, were identified to be main capping sites of red AuNCs. Peptides containing oxidized cysteines (sulfinic or cysteic acid) were identified as reducing sites mainly in the non-core fraction, suggesting that disulfide cleavages by oxidization and conformational changes contributed to the subsequent growth of nanoclusters at nearby intact disulfide pairs. This is the first report on precise identification of the reducing and capping sites of BSA-AuNCs.

Sign in / Sign up

Export Citation Format

Share Document