Molecular Mass Measurement of Hydrophobic and Aggregative Virus Proteins to Confirm Sequence Variation and Post-translational Modification by Electrospray Ionization and Array Detection.

1996 ◽  
Vol 44 (6) ◽  
pp. 641-652
Author(s):  
Keiichiro ISHIKAWA ◽  
Toshihiro OMURA ◽  
Yoshinori KOGA ◽  
Yoshio NIWA ◽  
Masahiko TSUCHIYA
Keyword(s):  
Molecular Mass ◽  
Electrospray Ionization ◽  
Sequence Variation ◽  
Mass Measurement ◽  
Post Translational Modification ◽  
Array Detection ◽  
Molecular Mass Measurement ◽  
Virus Proteins

NMR Measure of Translational Diffusion and Fractal Dimension. Application to Molecular Mass Measurement

2009 ◽  
Vol 113 (7) ◽  
pp. 1914-1918 ◽  
Author(s):  
Sophie Augé ◽  
Pierre-Olivier Schmit ◽  
Christopher A. Crutchfield ◽  
Mohammad T. Islam ◽  
Douglas J. Harris ◽  
...  
Keyword(s):  
Fractal Dimension ◽  
Molecular Mass ◽  
Mass Measurement ◽  
Translational Diffusion ◽  
Molecular Mass Measurement

Parallel Accelerator and Molecular Mass Measurement of Carbon-14-Labeled Analytes

2021 ◽  
pp. 1-10
Author(s):  
Benjamin J. Stewart ◽  
Ted J. Ognibene
Keyword(s):  
Molecular Mass ◽  
Mass Measurement ◽  
Carbon 14 ◽  
Molecular Mass Measurement

scholarly journals Molecular mass measurement of polymerase chain reaction products amplified from human blood dna by electrospray ionization mass spectrometry

1995 ◽  
Vol 9 (15) ◽  
pp. 1484-1486 ◽  
Author(s):  
Yasuhiro Naito ◽  
Keiichiro Ishikawa ◽  
Yoshinori Koga ◽  
Toshihiro Tsuneyoshi ◽  
Hideya Terunuma ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Polymerase Chain Reaction ◽  
Electrospray Ionization ◽  
Human Blood ◽  
Mass Measurement ◽  
Ionization Mass ◽  
Reaction Products ◽  
Chain Reaction ◽  
Polymerase Chain ◽  
Molecular Mass Measurement

scholarly journals Precise Molecular Mass Measurement of Polymers

Kobunshi ◽  
1995 ◽  
Vol 44 (7) ◽  
pp. 450-450
Author(s):  
Keiichiro ISHIKAWA
Keyword(s):  
Molecular Mass ◽  
Mass Measurement ◽  
Molecular Mass Measurement

ExtensiveDe NovoSequencing of New Parvalbumin Isoforms Using a Novel Combination of Bottom-Up Proteomics, Accurate Molecular Mass Measurement by FTICR−MS, and Selected MS/MS Ion Monitoring

2010 ◽  
Vol 9 (9) ◽  
pp. 4393-4406 ◽  
Author(s):  
Mónica Carrera ◽  
Benito Cañas ◽  
Jesús Vázquez ◽  
José M. Gallardo
Keyword(s):  
Molecular Mass ◽  
Mass Measurement ◽  
Bottom Up ◽  
Fticr Ms ◽  
Molecular Mass Measurement

scholarly journals Extra-platelet low-molecular-mass thiols mediate the inhibitory action of S-nitrosoalbumin on human platelet aggregation via S-transnitrosylation of the platelet surface

Amino Acids ◽  
2021 ◽  
Author(s):  
Dimitrios Tsikas
Keyword(s):  
Platelet Aggregation ◽  
Molecular Mass ◽  
Underlying Mechanism ◽  
Selective Extraction ◽  
Post Translational Modification ◽  
No Donor ◽  
Platelet Surface ◽  
Sh Groups ◽  
Human Platelet Aggregation ◽  
Inhibitory Potential

AbstractNitrosylation of sulfhydryl (SH) groups of cysteine (Cys) moieties is an important post-translational modification (PTM), often on a par with phosphorylation. S-Nitrosoalbumin (ALB-Cys34SNO; SNALB) in plasma and S-nitrosohemoglobin (Hb-Cysβ93SNO; HbSNO) in red blood cells are considered the most abundant high-molecular-mass pools of nitric oxide (NO) bioactivity in the human circulation. SNALB per se is not an NO donor. Yet, it acts as a vasodilator and an inhibitor of platelet aggregation. SNALB can be formed by nitrosation of the sole reduced Cys group of albumin (Cys34) by nitrosating species such as nitrous acid (HONO) and nitrous anhydride (N2O3), two unstable intermediates of NO autoxidation. SNALB can also be formed by the transfer (S-transnitrosylation) of the nitrosyl group (NO+) of a low-molecular-mass (LMM) S-nitrosothiol (RSNO) to ALB-Cys34SH. In the present study, the effects of LMM thiols on the inhibitory potential of ALB-Cys34SNO on human washed platelets were investigated. ALB-Cys34SNO was prepared by reacting n-butylnitrite with albumin after selective extraction from plasma of a healthy donor on HiTrapBlue Sepharose cartridges. ALB-Cys34SNO was used in platelet aggregation measurements after extended purification on HiTrapBlue Sepharose and enrichment by ultrafiltration (cutoff, 20 kDa). All tested LMM cysteinyl thiols (R-CysSH) including l-cysteine and L-homocysteine (at 10 µM) were found to mediate the collagen-induced (1 µg/mL) aggregation of human washed platelets by SNALB (range, 0–10 µM) by cGMP-dependent and cGMP-independent mechanisms. The LMM thiols themselves did not affect platelet aggregation. It is assumed that the underlying mechanism involves S-transnitrosylation of SH groups of the platelet surface by LMM RSNO formed through the reaction of SNALB with the thiols: ALB-Cys34SNO + R-CysSH ↔ ALB-Cys34SH + R-CysSNO. Such S-transnitrosylation reactions may be accompanied by release of NO finally resulting in cGMP-dependent and cGMP-independent mechanisms.

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