Table 3.
Fraction | Accession | Gene name | Description | MOWSE | Peptides Matched | Example Peptides |
---|---|---|---|---|---|---|
3 | EEE22451 | Putative uncharacterized protein | 837 | 7 | K.LEVGETCTIEMLPQNSK.V; K.HKLEVGETCTIEMLPQNSK.V | |
3 | EEE23072 | Putative uncharacterized protein | 194 | 4 | R.ATVHPGDTVTMQCPGAISSNPADVSK.Y; R.LILDIEKSEEEVVR.T | |
3 | EEE32684 | Surface protein rhoptry protein | 135 | 2 | K.SQANQGSPLPPPRPNLLR.R; R.GLMSGVGWVK.R |
|
3 | EEE29336 | Histone H4 | 110 | 2 | R.ISGLIYEEIR.G; R.DNIQGITKPAIR.R |
|
3 | XP_002370897 | ROP 2 | Rhoptery protein 2 | 91 | 3 | R.DSGDVILEELFK.R; K.GPSAIVFEATDR.E |
3 | EEE23774 | Ribosomal protein S8 | 82 | 2 | K.NSIVAIDATPFK.A; K.LDPLLEEQFNTGR.L |
|
4 | AAD38419 | HSP 60 | 283 | 4 | K.QVASTTNDIAGDGTTTATLLAR.A; K.TLTHELELVEGLK.F | |
4 | XP_002369317 | Proteasome subunit alpha (Type 2) | 215 | 7 | R.YNPDIELEDAIHTAILTLK.E; K.EGFEGAMNEHNIEIGVVGEDR.K + Oxidation (M) | |
4 | EEE23454 | Proteasome subunit alpha (Type 1) | 182 | 3 | K.ELSLDEIQALLDK.M; R.NFESFPGLSPEELELHAMK.A | |
4 | XP_002366589 | Proteasome subunit alpha (Type 4) | 162 | 4 | K.EDLDVDAALLLAAK.V; K.QEWKEDLDVDAALLLAAK.V | |
4 | EEE19215 | Proteasome subunit Beta [(Type 7) | 100 | 2 | K.GCAVVLGGVDFK.G; R.VSMAVSVLSQELFK.Y |
|
4 | EEE25357 | Proteasome subunit alpha (Type 7) | 129 | 2 | K.DLVVLAVEK.K; R.LNTATAPSVDYIAK.F |
|
5 | EEE30125 | Cytosol aminopeptidase putative | 142 | 2 | K.LTLFTDDVEAVNR.S R.VVTSFLETLLVELQPDLR.F |
Proteins were identified in each fraction by blasting the results of the peptide analysis versus the N. caninum and T. gondii genomic.
Proteins were identified in each fraction by blasting the results of the peptide analysis versus the N. caninum and T. gondii genomic databases. Table 1 lists protein identified from the N. caninum database; Table 2 T. gondii homologues identified in more than one fraction and Table 3 T. gondii homologues present only in one of the three fractions. MOWSE scores (for Molecular Weight Search) indicate the likelihood of having correctly identified a specific protein from the molecular weight of the peptides created by its proteolytic digestion and measured with mass spectrometry. The dot (.) in the peptide sequence denotes trypsin cleavage sites.