| First Author | Palm L | Year | 1996 |
| Journal | Int J Biochem Cell Biol | Volume | 28 |
| Issue | 12 | Pages | 1319-26 |
| PubMed ID | 9022290 | Mgi Jnum | J:38738 |
| Mgi Id | MGI:86120 | Doi | 10.1016/s1357-2725(96)00090-8 |
| Citation | Palm L, et al. (1996) Identification of five hemoglobins in B6C3F1 mice by mass spectrometry and sequence analysis. Int J Biochem Cell Biol 28(12):1319-26 |
| abstractText | The aim of the work is to identify and characterize the hemoglobins found in B6C3F1 mice using mass spectrometry. The primary structures are compared to those reported for BALB/c mice. Individual hemoglobin chains were isolated by reverse-phase high performance liquid chromatography (RP-HPLC). The molecular masses of the globins were determined using electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). The purified globin chains were enzymatically cleaved and the resulting peptides were separated by RP-HPLC. The chains were identified by N-terminal sequencing and mass spectrometry (MALDI). Selected peptides were analysed by Edman degradation. ESI analysis indicates that B6C3F1 mice have two alpha-globin chains (alpha-1 and alpha-2) and at least three beta-globin chains, beta-1, beta-2 and beta-3. This is one additional alpha- and one additional beta-globin chain than reported in the literature for BALB/c mice. Mass and sequence analysis of enzymatically generated peptides showed variations in the amino acid sequence in the alpha-1, alpha-2, beta-2 and beta-3 chains compared to the BALB/c mouse hemoglobins (alpha, beta (minor) and beta (major)). The study showed that mass spectrometry in combination with traditional protein chemistry is able to identify and locate minor protein sequence variations. |
