Efficiency of Trypsin Digestion for Mass-Spectrometry-Based Identification and Quantification of Oxidized Proteins: Evaluation of the Digestion of Oxidized Bovine Serum Albumin

2014 ◽  
Vol 20 (3) ◽  
pp. 271-278 ◽  
Author(s):  
Duarte D. Gouveia ◽  
André M.N. Silva ◽  
Rui Vitorino ◽  
M. Rosário M. Domingues ◽  
Pedro Domingues
Keyword(s):  
Mass Spectrometry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Trypsin Digestion ◽  
Oxidized Proteins ◽  
Identification And Quantification

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

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.

Antimutagenic activity of whole casein on the pepper-induced mutagenicity to streptomycin-dependent strain SD 510 of Salmonella typhimurium TA 98

1988 ◽  
Vol 55 (3) ◽  
pp. 435-442 ◽  
Author(s):  
Akiyoshi Hosono ◽  
Kunigal N. Shashikanth ◽  
Hajime Otani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Salmonella Typhimurium ◽  
Bovine Serum ◽  
Trypsin Digestion ◽  
Antimutagenic Activity ◽  
Temperature Dependent ◽  
Egg Albumin ◽  
Dependent Strain ◽  
Papain Digestion

SummaryWhen the antimutagenic activity of milk or cultured milk components on the pepper-induced mutagenicity to streptomycin-dependent strain SD 510 of Salmonella typhimurium TA 98 was investigated, whole casein showed a significant antimutagenic activity. Heating at 121 °C for 15 min completely destroyed the antimutagenic activity of casein, which was temperature dependent. While acid or papain digestion resulted in the loss of antimutagenic activity of casein, trypsin digestion had little effect although the digestion of casein by each proteinase was over 75%. β-Casein, egg albumin, and bovine serum albumin also had a similar antimutagenic activity to that of whole casein.

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