scholarly journals In VivoPhosphorylation Site Mapping in Mouse Cardiac Troponin I by High Resolution Top-Down Electron Capture Dissociation Mass Spectrometry: Ser22/23 Are the Only Sites Basally Phosphorylated

Biochemistry ◽  
2009 ◽  
Vol 48 (34) ◽  
pp. 8161-8170 ◽  
Author(s):  
Serife Ayaz-Guner ◽  
Jiang Zhang ◽  
Lin Li ◽  
Jeffery W. Walker ◽  
Ying Ge
2006 ◽  
Vol 52 (2) ◽  
pp. 212-219 ◽  
Author(s):  
David M Bunk ◽  
Michael J Welch

Abstract Background: To address the continuing need for the standardization of clinical human cardiac troponin I (cTnI) assays, NIST, with the assistance of the AACC/IFCC Cardiac Troponin I Standardization Committee, has developed a new certified reference material, Standard Reference Material (SRM) 2921: Human Cardiac Troponin Complex. Methods: The concentration of cTnI in SRM 2921 was determined through a combination of reversed-phase liquid chromatography (LC) with ultraviolet detection and amino acid analysis. Characterization of the intact troponin subunits was accomplished through reversed-phase LC coupled with mass spectrometry. Posttranslational modifications to the cTnI in SRM 2921 were investigated by combining proteolytic digestion with matrix-assisted laser desorption/ionization mass spectrometry. Additionally, reference concentration values for cTnT and cTnC were also determined. Results: The concentration of human cTnI in SRM 2921 is 31.2 (1.4) mg/L (where 1.4 mg/L is the uncertainty at a 95% level of confidence), as certified through a method that provides traceability to the International System of Units (SI). Reference concentration values of the cTnT and cTnC subunits were determined to be 36.9 (3.8) mg/L and 24.2 (1.3) mg/L, respectively. Conclusions: This first cTnI reference material should provide SI traceability to clinical cTnI assays once commutability has been validated, and could assist in the international harmonization of cTnI assays as a tool for understanding the underlying causes of interassay variability.


2015 ◽  
Vol 17 (16) ◽  
pp. 10538-10550 ◽  
Author(s):  
Sophie R. Harvey ◽  
Massimiliano Porrini ◽  
Robert C. Tyler ◽  
Cait E. MacPhee ◽  
Brian F. Volkman ◽  
...  

Ion mobility mass spectrometry can be combined with data from top-down sequencing to discern adopted conformations of proteins in the absence of solvent.


2011 ◽  
Vol 10 (9) ◽  
pp. 4054-4065 ◽  
Author(s):  
Jiang Zhang ◽  
Moltu J. Guy ◽  
Holly S. Norman ◽  
Yi-Chen Chen ◽  
Qingge Xu ◽  
...  

2011 ◽  
Vol 22 (8) ◽  
pp. 1432-1440 ◽  
Author(s):  
David J. Clarke ◽  
Euan Murray ◽  
Ted Hupp ◽  
C. Logan Mackay ◽  
Pat R. R. Langridge-Smith

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