The adsorption of carbon dioxide by tertiary alkanolamines

1999 ◽  
Vol 77 (3) ◽  
pp. 401-408 ◽  
Author(s):  
M. Teresa SR Gomes ◽  
Cristina MF Barros ◽  
M Graça O. Santana-Marques ◽  
João ABP Oliveira
Keyword(s):  
Mass Spectrometry ◽  
Carbon Dioxide ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Fast Atom Bombardment ◽  
Resonance Spectroscopy ◽  
Quartz Crystals ◽  
Piezoelectric Quartz ◽  
Gaseous Carbon Dioxide ◽  
Mass Spectrometry Mass Spectrometry

The quantification of gaseous carbon dioxide, CO2, adsorbed by tertiary alkanolamines was performed using a quartz crystal microbalance. Carbon dioxide was injected over piezoelectric quartz crystals coated with different amounts of N,N,N',N'-tetrakis(2-hydroxyethyl)ethylenediamine (THEED), N,N,N',N'-tetrakis(2-hydroxypropyl)ethyl enediamine (Quadrol), and triethanolamine (TEA), and the frequency decrease of the crystals was recorded. The nature of the interaction of the alkanolamines with CO2 was investigated by nuclear magnetic resonance spectroscopy (NMR), Fourier transform infrared spectroscopy (FTIR), fast atom bombardment mass spectrometry (FABMS), and mass spectrometry/mass spectrometry (MS/MS).Key words: alkanolamine, quartz crystal microbalance, piezoelectric quartz crystal.

scholarly journals Rapid and Simultaneous Quantification of 4 Urinary Proteins by Piezoelectric Quartz Crystal Microbalance Immunosensor Array

2006 ◽  
Vol 52 (12) ◽  
pp. 2273-2280 ◽  
Author(s):  
Yang Luo ◽  
Ming Chen ◽  
Qianjun Wen ◽  
Meng Zhao ◽  
Bo Zhang ◽  
...  
Keyword(s):  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Clinical Chemistry ◽  
Label Free ◽  
Urinary Proteins ◽  
Quartz Crystals ◽  
Piezoelectric Quartz ◽  
Piezoelectric Immunosensor ◽  
Highly Sensitive ◽  
Piezoelectric Quartz Crystal

Abstract Background: Urinary proteins are predictive and prognostic markers for diabetes nephropathy. Conventional methods for the quantification of urinary proteins, however, are time-consuming, and most require radioactive labeling. We designed a label-free piezoelectric quartz crystal microbalance (QCM) immunosensor array to simultaneously quantify 4 urinary proteins. Methods: We constructed a 2 × 5 model piezoelectric immunosensor array fabricated with disposable quartz crystals for quantification of microalbumin, α1-microglobulin, β2-microglobulin, and IgG in urine. We made calibration curves after immobilization of antibodies at an optimal concentration and then evaluated the performance characteristics of the immunosensor with a series of tests. In addition, we measured 124 urine samples with both QCM immunosensor array and immunonephelometry to assess the correlation between the 2 methods. Results: With the QCM immunosensor array, we were able to quantify 4 urinary proteins within 15 min. This method had an analytical interval of 0.01–60 mg/L. The intraassay and interassay imprecisions (CVs) were <10%, and the relative recovery rates were 90.3%–109.1%. Nonspecificity of the immunosensor was insignificant (frequency shifts <20 Hz). ROC analyses indicated sensitivities were ≥95.8% and, specificities were ≥76.3%. Bland–Altman difference plots showed the immunosensor array to be highly comparable to immunonephelometry. Conclusions: The QCM system we designed has the advantages of being rapid, label free, and highly sensitive and thus can be a useful supplement to commercial assay methods in clinical chemistry.

scholarly journals Unraveling cardiolipin-induced conformational change of cytochrome c through H/D exchange mass spectrometry and quartz crystal microbalance

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu
Keyword(s):  
Mass Spectrometry ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Interaction Model ◽  
Moderate Increase ◽  
Exchange Mass Spectrometry ◽  
Mitochondrial Regulation ◽  
Crucial Component ◽  
Drastic Increase ◽  
Hydrogen Deuterium

AbstractCardiolipin (CL), a crucial component in inner mitochondrial membranes, interacts with cytochrome c (cyt c) to form a peroxidase complex for the catalysis of CL oxidation. Such interaction is pivotal to the mitochondrial regulation of apoptosis and is affected by the redox state of cyt c. In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Upon association with CL, ferrous cyt c resulted in a moderate increase in deuteration, whereas the ferric form caused a drastic increase of deuteration, which indicated that CL-bound ferric cyt c formed an extended conformation. These results were consistent with those of the frequency (f) − dissipation (D) experiments, which revealed that ferric cyt c yielded greater values of |ΔD/Δf| within the first minute. Further fragmentation analysis based on HDXMS indicated that the effect of CL binding was considerably different on ferric and ferrous cyt c in the C-helix and the Loop 9–24. In ferric cyt c, CL binding affected Met80 and destabilized His18 interaction with heme, which was not observed with ferrous cyt c. An interaction model was proposed to explain the aforementioned results.

SURFACE PLASMON RESONANCE SPECTROSCOPY AND QUARTZ CRYSTAL MICROBALANCE STUDY OF PROTEIN-DNA INTERACTIONS IN HORMONE RECEPTOR BIOLOGY

COSMOS ◽  
2009 ◽  
Vol 05 (01) ◽  
pp. 79-95
Author(s):  
XIAODI SU
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Quartz Crystal Microbalance ◽  
Conformational Changes ◽  
Plasmon Resonance ◽  
Quartz Crystal ◽  
Resonance Spectroscopy ◽  
Dna Interactions ◽  
Protein Dna Interactions

Surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance (QCM) are surface sensitive analytical techniques capable of real-time monitoring of biomolecular interactions. In this article we review our past work on the use of these two techniques for studying protein–DNA interactions, exemplified with estrogen receptors (ER) and their response elements (ERE). Various assay schemes have been developed for a comprehensive characterization of ER–ERE interactions in terms of sequence specificity, binding affinity, stoichiometry, ligand effects on binding dynamics and conformational changes in the proteins and DNA. These are all important characteristics underlining the mechanism of ER-mediated gene transcription. With these studies we have made the following demonstrations to describe the advantages of these two techniques, namely (i) SPR technique is superior and more versatile than conventional (electrophoretic mobility shift assay) EMSA for studying protein-DNA interactions; (ii) QCM is an alternative tool for studying conformational changes in protein–DNA complexes and (iii) combinational SPR and QCM analysis provides additional characterization of biomolecular films, e.g. film thickness, water content, and conformation rigidity etc.

Sign in / Sign up

Export Citation Format

Share Document