scholarly journals Trypsin/Lys-C protease mix for enhanced protein mass spectrometry analysis

2013 ◽  
Vol 10 (11) ◽  
pp. i-ii ◽  
Author(s):  
Sergei Saveliev ◽  
Mark Bratz ◽  
Roman Zubarev ◽  
Matt Szapacs ◽  
Harshavardhan Budamgunta ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Protein Mass ◽  
Protein Mass Spectrometry

scholarly journals Antigens from H22 cell mutation induced by lentinan are correlated with HCC immunoprophylaxis

2020 ◽  
Author(s):  
Xin Yang ◽  
Yandong Li ◽  
Wen Wang ◽  
Chong Li ◽  
Dandan Zhao ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
T Cells ◽  
Liver Cancer ◽  
Tumor Cells ◽  
Cd8 T Cells ◽  
Specific Antigen ◽  
Mass Spectrometry Analysis ◽  
T Lymphocyte Subsets ◽  
Spectrometry Analysis ◽  
Protein Mass

Abstract Background Lentinan can inhibit the proliferation of many kinds of tumor cells, and some studies have shown that lentinan can inhibit the growth of tumor tissue by directly killing tumor cells. The purpose of this study was to investigate the immunoprophylaxis effect and mechanism of tumor specific antigen induced by lentinan on liver cancer in mice.Methods The immunogen was prepared which was induced by lentinan. And two different mouse H22 liver cancer models (ascites tumor and solid tumor)were established after immunogen immunized. The tumor growth and immune organ index of mice in each group were measured. In order to analyze the immune mechanism, the activity of CTL cells, activation of ADCC pathway ,T lymphocyte subsets, expression of CD4 + T,CD8 + T cells and expression of DC, and surface molecular markers CD80 and CD86 in immunized mice were analyzed. The expression of cytokines such as IFN-γ and TNF-α in serum and cell supernatant of mice in each group was tested too. Finally, the immunogen was analyzed by Liquid Chromatography-Mass Spectrometry (LC-MS), and the functional proteins were screened for further analysis.Results The liver, spleen and thymus of the mice immunized with immunogen were protected to a certain extent. In immunized mice, the proportion of CD4 + T cells increased, the proportion of CD8 + T cells decreased, the ratio of CD4 + T/CD8 + T increased, and the killing activity of T lymphocytes increased significantly. The expression of CD80 in mature DC cells of immunized mice increased and cytokines increased significantly. The results of protein mass spectrometry analysis of immunogen showed that immunogen produced protein properties that inhibit cancer.Conclusion The H22 whole-cell cleavage vaccine induced by lentinan is effective in the immunity of mouse hepatoma H22 and has development value in the future.

Mass Spectrometry-Based Proteomic Approach in Juglans regia

2021 ◽  
Vol 885 ◽  
pp. 25-31
Author(s):  
Donatella Aiello
Keyword(s):  
Mass Spectrometry ◽  
Juglans Regia ◽  
Maldi Mass Spectrometry ◽  
Mass Spectrometry Analysis ◽  
Intact Protein ◽  
Protein Fractionation ◽  
Spectrometry Analysis ◽  
Protein Mass ◽  
Proteomic Approach ◽  
Mass Information

We proposed a MALDI mass spectrometry based approach to characterize walnut allergens. The strategy is based on the extraction of hydro-soluble tissue proteins followed by protein fractionation and mass-spectrometry analysis. Linear MALDI was adopted to evaluate the intact protein mass information and the presence of glycoproteins.

scholarly journals Effect of Ocular Hypertension on D-β-Aspartic Acid-Containing Proteins in the Retinas of Rats

2019 ◽  
Vol 2019 ◽  
pp. 1-8 ◽  
Author(s):  
Takashi Kanamoto ◽  
Takashi Tachibana ◽  
Yasushi Kitaoka ◽  
Toshio Hisatomi ◽  
Yasuhiro Ikeda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ocular Hypertension ◽  
Aspartic Acid ◽  
Atp Synthase ◽  
Wistar Rats ◽  
Protein Band ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Sds Page

Purpose. To investigate the effect of ocular hypertension-induced isomerization of aspartic acid in retinal proteins. Methods. Adult Wistar rats with ocular hypertension were used as an experimental model. D-β-aspartic acid-containing proteins were isolated by SDS-PAGE and western blot with an anti-D-β-aspartic acid antibody and identified by liquid chromatography-mass spectrometry analysis. The concentration of ATP was measured by ELISA. Results. D-β-aspartic acid was expressed in a protein band at around 44.5 kDa at much higher quantities in the retinas of rats with ocular hypertension than in those of normotensive rats. The 44.5 kDa protein band was mainly composed of α-enolase, S-arrestin, and ATP synthase subunits α and β, in both the ocular hypertensive and normotensive retinas. Moreover, increasing intraocular pressure was correlated with increasing ATP concentrations in the retinas of rats. Conclusion. Ocular hypertension affected the expression of proteins containing D-β-aspartic acid, including ATP synthase subunits, and up-regulation of ATP in the retinas of rats.

scholarly journals N-Terminomics Strategies for Protease Substrates Profiling

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4699
Author(s):  
Mubashir Mintoo ◽  
Amritangshu Chakravarty ◽  
Ronak Tilvawala
Keyword(s):  
Mass Spectrometry ◽  
Protease Activity ◽  
Viral Infections ◽  
Mass Spectrometry Analysis ◽  
Post Translational Modification ◽  
Spectrometry Analysis ◽  
Physiological Conditions ◽  
Inflammatory Conditions ◽  
Biological Mixtures

Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by protease activation, activity, and substrate specificity. Thus, identifying protease substrates and proteolytic events under physiological conditions can provide crucial information about how the change in protease regulation can alter the cellular proteolytic landscape. In recent years, mass spectrometry-based techniques called N-terminomics have become instrumental in identifying protease substrates from complex biological mixtures. N-terminomics employs the labeling and enrichment of native and neo-N-termini peptides, generated upon proteolysis followed by mass spectrometry analysis allowing protease substrate profiling directly from biological samples. In this review, we provide a brief overview of N-terminomics techniques, focusing on their strengths, weaknesses, limitations, and providing specific examples where they were successfully employed to identify protease substrates in vivo and under physiological conditions. In addition, we explore the current trends in the protease field and the potential for future developments.

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