Table 2.
Protein No. | Identification | Identified peptides | Coverage % | pI | Mr (kDa) | Function | Swiss-Prot Accession Number |
15 | ND* | ||||||
23 | ND | ||||||
28 | Triosephosphate isomerase | IAVAAQNCYK (59–68) TATPQQAQEVHEK (175–187) TATPQQAQEVHEKLR (175–189) SNVSDAVAQSTR (194–205) IIYGGSVTGATCK (206–218) |
20 | 7.1 | 26.89 | Enzyme | P60174 |
36 | αA-crystallin | RTLGPFYPSR (12–21) TLGPFYPSR (13–21) TVLDSGISEVR (55–65) QDDHGYISR (104–112) IQTGLDATHAER (146–157) AIPVSREEKPTSAPSS (158–173) |
33 | 5.8 | 20.01 | Chaperone | P02489 |
48 | β-tubulin (C-terminal fragment) | NSSYFVEWIPNNVK (119–132) TAVCDIPPR (133–141) RISEQFTAMFR (162–172) ISEQFTAMFRR (163–173) |
11 | 4.9 | 26.03 | Cytoskeletal | P68371 |
52 | ATP synthase β-subunit precursor (N-terminal fragment) | LVLEVAQHLGESTVR (95–109) TIAMDGTEGLVR (110–121) VLDSGAPIKIPVGPETLGR (125–143) IMNVIGEPIDER (144–155) |
11 | 5.3 | 56.54 | Oxidative phosphorylation | P06576 |
55 | ND |
* ND, not determined.
† Spectra obtained by MALDI-TOF were used to search the Swiss-Prot databases. The peptides given were in agreement with measured masses. Number in parentheses indicate the position of the peptide in the protein.