Table 1. Identification of proteins from mouse kidney peroxisomes using MALDI–TOF-MS.
Protein spots derived from the two-dimensional gel were prepared for MALDI–TOF-MS analysis as described in the Experimental section. The resulting peptide spectra were used to search a non-redundant protein sequence database (Swiss-Prot/TrEMBL) using the Proteinprobe program or the MASCOT search engine and database. The molecular mass of the denatured proteins was calculated from their primary amino acid sequence as taken from the GenBank® database. DHAP, dihydroxyacetonephosphate.
| Molecular mass (kDa) | ||||
|---|---|---|---|---|
| No. | Identified protein | Native | Denatured | Remarks |
| 1 | Catalase | 240 | 59.8 | Homotetramer [17] |
| 2 | Acyl-CoA oxidase I | 140 | 74.6 | Homodimer [16] |
| 3 | L-Hydroxyacid oxidase 2 | 140–240 | 38.8 | Homomultimer |
| 4 | α-Methylacyl-CoA racemase | ∼80 | 41.7 | Homodimer |
| 5 | RP2p | <50 | 40.4 | Accession number P11930 |
| 6 | D-Amino acid oxidase | <50 | 38.7 | Monomer |
| 7 | trans-2-enoyl-CoA reductase | ∼30/∼60 | 32.5 | Monomer and homodimer |
| 8 | Epoxide hydrolase | ∼70 | 62.5 | Accession number P34914 |
| 9 | Peroxisomal bifunctional enzyme | ∼80/∼160 | 78.2 | Monomer and oligomer |
| 10 | Acyl-CoA oxidase 3 | >100 | 78.4 | Homodimer |
| 11 | Δ3,Δ2-Enoyl-CoA isomerase | <50 | 35.2 | Riken 1810022C23 gene |
| 12 | Alkyl-DHAP synthase | ∼70 | 71.7 (67.0) | Precursor (mature form) |
| 13 | Carnitine O-octanoyltransferase | ∼80 | 70.3 | Accession number P11466 |