Abstract
The identification of modification tri-methylation and acetylation sites of histone H3 was investigated by mass spectrometry. Histone H3 was purified by HPLC from the core histones isolated from chicken erythrocytes, digested by trypsin and then analyzed by MALDI-TOF and tandem spectrometry. High mass accuracy (5ppm) MALDI-TOF mass measurements were used to detect the mass difference (0.0360 Da, 40 ppm) between the substitution of Lys of an acetyl group (42.0106) versus three methyl groups (42.0470). The results show that H3 lysine 9 is mono-, di- and tri-methylated, and none of the MS evidence supports a putative acetylation of histone lysine 9 in chicken erythrocytes.
| Original language | English (US) |
|---|---|
| Title of host publication | Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics |
| Pages | 315-316 |
| Number of pages | 2 |
| State | Published - 2002 |
| Externally published | Yes |
| Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Other
| Other | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
|---|---|
| Country | United States |
| City | Orlando, FL |
| Period | 6/2/02 → 6/6/02 |
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ASJC Scopus subject areas
- Spectroscopy
Cite this
Differentiation of tri-methylation from acetylation of histone H3 lysine 9 by mass spectrometry. / Zhang, Kangling; Yau, Peter M.; Jones, Patrick R.
Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. 2002. p. 315-316.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - Differentiation of tri-methylation from acetylation of histone H3 lysine 9 by mass spectrometry
AU - Zhang, Kangling
AU - Yau, Peter M.
AU - Jones, Patrick R.
PY - 2002
Y1 - 2002
N2 - The identification of modification tri-methylation and acetylation sites of histone H3 was investigated by mass spectrometry. Histone H3 was purified by HPLC from the core histones isolated from chicken erythrocytes, digested by trypsin and then analyzed by MALDI-TOF and tandem spectrometry. High mass accuracy (5ppm) MALDI-TOF mass measurements were used to detect the mass difference (0.0360 Da, 40 ppm) between the substitution of Lys of an acetyl group (42.0106) versus three methyl groups (42.0470). The results show that H3 lysine 9 is mono-, di- and tri-methylated, and none of the MS evidence supports a putative acetylation of histone lysine 9 in chicken erythrocytes.
AB - The identification of modification tri-methylation and acetylation sites of histone H3 was investigated by mass spectrometry. Histone H3 was purified by HPLC from the core histones isolated from chicken erythrocytes, digested by trypsin and then analyzed by MALDI-TOF and tandem spectrometry. High mass accuracy (5ppm) MALDI-TOF mass measurements were used to detect the mass difference (0.0360 Da, 40 ppm) between the substitution of Lys of an acetyl group (42.0106) versus three methyl groups (42.0470). The results show that H3 lysine 9 is mono-, di- and tri-methylated, and none of the MS evidence supports a putative acetylation of histone lysine 9 in chicken erythrocytes.
UR - http://www.scopus.com/inward/record.url?scp=2442635424&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=2442635424&partnerID=8YFLogxK
M3 - Conference contribution
AN - SCOPUS:2442635424
SP - 315
EP - 316
BT - Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
ER -