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) |
|---|---|
| Pages | 315-316 |
| Number of pages | 2 |
| State | Published - Dec 1 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 |
ASJC Scopus subject areas
- Spectroscopy
Fingerprint Dive into the research topics of 'Differentiation of tri-methylation from acetylation of histone H3 lysine 9 by mass spectrometry'. Together they form a unique fingerprint.
Cite this
Zhang, K., Yau, P. M., & Jones, P. R. (2002). Differentiation of tri-methylation from acetylation of histone H3 lysine 9 by mass spectrometry. 315-316. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.