A new approach, based on the use of atmospheric pressure chemical ionization ion trap mass spectrometry (APCI-ITMS), but without a corona discharge, was investigated for application to creating and monitoring protein ions. It must be emphasized that APCI is not usually used in protein analysis. In order to verify the applicability of the proposed method to the analysis of proteins, two standard proteins (horse cytochrome c and horse myoglobin) were analyzed. A mixture of the two proteins was also analyzed showing that this novel approach, based on the use of APCI, can be used in the analysis of protein mixtures
Development of mass spectrometry techniques to detect protein oxidation, which contributes to signal...
While allowing analysis of intact proteins without a theoretical upper mass limit, the Orbitrap mass...
A simple procedure is described that increases sensitivity and dynamic range for the analysis of a p...
A novel approach, based on the use of atmospheric pressure chemical ionization ion trap mass spectr...
In a typical bottom-up proteomics workflow, proteins are enzymatically cleaved, and the resulting pe...
The identification of proteins separated on two-dimensional gels is most commonly performed by tryps...
Paper spray (PS) ionization, an ambient ionization method, has previously been explored as a direct ...
We demonstrate a method for determining the collision cross-sections (CCSs) of protein ions based on...
‘Top down’ protein analysis has been extended to ion trap mass spectrometry via the use of ion/ion p...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. An ion source oper...
Quantitative analysis with mass spectrometric detection is no longer limited to small molecules. A n...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. Such low-pressure ...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. An ion source oper...
Laserspray ionization (LSI) mass spectrometry (MS) allows, for the first time, the analysis of prote...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. Such low-pressure ...
Development of mass spectrometry techniques to detect protein oxidation, which contributes to signal...
While allowing analysis of intact proteins without a theoretical upper mass limit, the Orbitrap mass...
A simple procedure is described that increases sensitivity and dynamic range for the analysis of a p...
A novel approach, based on the use of atmospheric pressure chemical ionization ion trap mass spectr...
In a typical bottom-up proteomics workflow, proteins are enzymatically cleaved, and the resulting pe...
The identification of proteins separated on two-dimensional gels is most commonly performed by tryps...
Paper spray (PS) ionization, an ambient ionization method, has previously been explored as a direct ...
We demonstrate a method for determining the collision cross-sections (CCSs) of protein ions based on...
‘Top down’ protein analysis has been extended to ion trap mass spectrometry via the use of ion/ion p...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. An ion source oper...
Quantitative analysis with mass spectrometric detection is no longer limited to small molecules. A n...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. Such low-pressure ...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. An ion source oper...
Laserspray ionization (LSI) mass spectrometry (MS) allows, for the first time, the analysis of prote...
Mass spectrometer ion sources are normally located inside a high-vacuum envelope. Such low-pressure ...
Development of mass spectrometry techniques to detect protein oxidation, which contributes to signal...
While allowing analysis of intact proteins without a theoretical upper mass limit, the Orbitrap mass...
A simple procedure is described that increases sensitivity and dynamic range for the analysis of a p...