Abstract
The curved-field reflectron (CFR), when used as the second mass analyzer in a tandem time-of-flight mass spectrometer, provides a design that enables the use of very high energy collision-induced dissociation (CID). Specifically, this is because the wide energy bandwidth of the CFR obviates the need for floating the collision region to decelerate the precursor ions and subsequently reaccelerating product ions to enable reflectron focusing. Here we describe the evolution of tandem instruments based on the CFR, from its introduction in 1993 to the current commercial TOF2 mass spectrometer from Shimadzu Corporation, and briefly review the history of TOF/TOF instruments. A number of applications are also described. One is the characterization of a C-terminal cleavage of cystatin C that appears to be associated with patients with remitting relapse multiple sclerosis (RRMS). Both surface-enhanced laser desorption/ionization (SELDI) and MALDI were used on a high performance TOF instrument operating in the MS and MS/MS modes. Tandem TOF mass spectrometry has also been used to determine the acetylation sites on histones and on the enzyme, histone acetyl transferase (HAT), responsible for the modification. Acetylation has been determined quantitatively for multiple sites on histone H3 and H4 using a deuteroacetylation method. For a number of closely spaced sites on the histone tail regions, MS/MS enables us to then determine both the order and distribution of acetylation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2-13 |
| Number of pages | 12 |
| Journal | Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences |
| Volume | 855 |
| Issue number | 1 SPEC. ISS. |
| DOIs | |
| State | Published - Aug 1 2007 |
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Keywords
- Acetylation
- Curved-field reflectron
- Cystatin
- Histone acetyl transferase (HAT)
- Histones
- Matrix-assisted laser desorption/ionization (MALDI)
- Multiple sclerosis
- Surface-enhanced laser desorption/ionization (SELDI)
- Tandem mass spectrometry
- Time-of-flight
ASJC Scopus subject areas
- Biochemistry
Cite this
Tandem time-of-flight (TOF/TOF) mass spectrometry and the curved-field reflectron. / Cotter, Robert J.; Griffith, Wendell; Jelinek, Christine.
In: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, Vol. 855, No. 1 SPEC. ISS., 01.08.2007, p. 2-13.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Tandem time-of-flight (TOF/TOF) mass spectrometry and the curved-field reflectron
AU - Cotter, Robert J.
AU - Griffith, Wendell
AU - Jelinek, Christine
PY - 2007/8/1
Y1 - 2007/8/1
N2 - The curved-field reflectron (CFR), when used as the second mass analyzer in a tandem time-of-flight mass spectrometer, provides a design that enables the use of very high energy collision-induced dissociation (CID). Specifically, this is because the wide energy bandwidth of the CFR obviates the need for floating the collision region to decelerate the precursor ions and subsequently reaccelerating product ions to enable reflectron focusing. Here we describe the evolution of tandem instruments based on the CFR, from its introduction in 1993 to the current commercial TOF2 mass spectrometer from Shimadzu Corporation, and briefly review the history of TOF/TOF instruments. A number of applications are also described. One is the characterization of a C-terminal cleavage of cystatin C that appears to be associated with patients with remitting relapse multiple sclerosis (RRMS). Both surface-enhanced laser desorption/ionization (SELDI) and MALDI were used on a high performance TOF instrument operating in the MS and MS/MS modes. Tandem TOF mass spectrometry has also been used to determine the acetylation sites on histones and on the enzyme, histone acetyl transferase (HAT), responsible for the modification. Acetylation has been determined quantitatively for multiple sites on histone H3 and H4 using a deuteroacetylation method. For a number of closely spaced sites on the histone tail regions, MS/MS enables us to then determine both the order and distribution of acetylation.
AB - The curved-field reflectron (CFR), when used as the second mass analyzer in a tandem time-of-flight mass spectrometer, provides a design that enables the use of very high energy collision-induced dissociation (CID). Specifically, this is because the wide energy bandwidth of the CFR obviates the need for floating the collision region to decelerate the precursor ions and subsequently reaccelerating product ions to enable reflectron focusing. Here we describe the evolution of tandem instruments based on the CFR, from its introduction in 1993 to the current commercial TOF2 mass spectrometer from Shimadzu Corporation, and briefly review the history of TOF/TOF instruments. A number of applications are also described. One is the characterization of a C-terminal cleavage of cystatin C that appears to be associated with patients with remitting relapse multiple sclerosis (RRMS). Both surface-enhanced laser desorption/ionization (SELDI) and MALDI were used on a high performance TOF instrument operating in the MS and MS/MS modes. Tandem TOF mass spectrometry has also been used to determine the acetylation sites on histones and on the enzyme, histone acetyl transferase (HAT), responsible for the modification. Acetylation has been determined quantitatively for multiple sites on histone H3 and H4 using a deuteroacetylation method. For a number of closely spaced sites on the histone tail regions, MS/MS enables us to then determine both the order and distribution of acetylation.
KW - Acetylation
KW - Curved-field reflectron
KW - Cystatin
KW - Histone acetyl transferase (HAT)
KW - Histones
KW - Matrix-assisted laser desorption/ionization (MALDI)
KW - Multiple sclerosis
KW - Surface-enhanced laser desorption/ionization (SELDI)
KW - Tandem mass spectrometry
KW - Time-of-flight
UR - http://www.scopus.com/inward/record.url?scp=34447567531&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34447567531&partnerID=8YFLogxK
U2 - 10.1016/j.jchromb.2007.01.009
DO - 10.1016/j.jchromb.2007.01.009
M3 - Article
C2 - 17258517
AN - SCOPUS:34447567531
VL - 855
SP - 2
EP - 13
JO - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
JF - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
SN - 1570-0232
IS - 1 SPEC. ISS.
ER -