Table 1.
Proteins identified in A. c. contortrix venom.
| Spot no. # | Identified Protein & | Accession * | Organism ¥ | Mass [kDa] £ | S ± | Peptide Sequence ¤ |
|---|---|---|---|---|---|---|
| 1 | Snake venom 5′-nucleotidase | V5NTD_CROAD | Crotalus adamanteus | 65.2 | 97 | ETPVLSNPEGPYLEFR (1719.099) |
| V5NTD_CROAD | Crotalus adamanteus | 65.2 | 39 | QAFEHSVHR (1110.651) | ||
| V5NTD_GLOBB | Gloydius blomhoffii blomhoffii | 6 | 115 | SFELTILHTNDVMAR (1753.091) | ||
| V5NTD_GLOBR | Gloydius brevicaudus | 65 | 65 | PMF SC 13.3% | ||
| 2 | l-amino-acid oxidase | OXLA_GLOHA | Gloydius halys | 57.4 | 116 | ETDYEEFLEIAR (1514.762) |
| OXLA_PSEAU | Pseudechis austarlis | 59 | 54 | PMS SC 10.4% | ||
| 3 | Beta-fibrinogenase brevinase | VSPB_GLOBL | Gloydius blomhoffii | 26.3 | 65 | VIGGDECNINEHR (1512.767) |
| Beta-fibrinogenase | VSPBF_MACLB | Macrovipera lebetina | 28.2 | 26 | FFCLSSK (888.452) | |
| 4 | Thrombin-like enzyme bilineobin | VSP2_AGKBI | Agkistrodon bilineatus | 27.1 | 64 | IIGGDECNINEHR (1526.785) |
| 28 | NSEHIAPLSLPSSPPIVGSVCR (2317.179) | |||||
| Thrombin-like enzyme asperase | VSPL_BOTAS | Bothrops asper | 28.6 | 118 | ETYPDVPHCANINILDHAVCR (2494.238) | |
| Snake venom serine protease PA | VSPP_TRIST | Trimeresurus stajnegri | 28.6 | 40 | VVLNEDEQIR (1115.567) | |
| Snake venom serine proteinase pallabin | VSP1_GLOHA | Gloydius halys | 29.3 | 27 | LDSPVKNSAHIAPLSLPSSPPVGSDCR (2888.600) | |
| Snake venom serine proteinase 9 | VSP9_CROAD | Crotalus adamanteus | 11.7 | 164 | ETYPDVPHCANINILDYEVCR (2578.230) | |
| Snake venom serine proteinase 12 | VSPC_CROAD | Crotalus adamanteus | 29.3 | 113 | DIMLIRLDSPVSNSEHIAPLSLPSSPPSVGSVCR (1823.985) | |
| Thrombin-like enzyme crotalase | VSPCR_CROAD | Crotalus adamanteus | 30.1 | 36 | WDKDIMLIR(1189.656) | |
| 5 | Protein C activator | VSPCA_AGKCO | Agkistrodon contortrix contortrix | 25.7 | 82 | PMF SC 34,2% |
| 91 | NSAHIAPLSLPSNPPSVGSVCR (2260.075) | |||||
| VSPCA_AGKBI | Agkistrodon bilineatus | 2.2 | 68 | VVGGDECNINEHR (1498.711) | ||
| 6 | Basic phospholipase A2 homolog | PA2HB_AGKPI | Agkistrodon piscivorus piscivorus | 14.7 | 80 | PMF SC 49% |
| Basic phospholipase A2 homolog MT1 | PA2H1_AGKCL | Agkistrodon contrortrix laticinctus | 16.5 | 80 | PMF SC 43% | |
| 7 | Cysteine-rich venom protein piscivorin | CRVP_AGKPI | Agkistrodon piscivorus piscivorus | 27.5 | 102 | MEHYPEAAANAER (1537.689) |
| 76 | MEHYPEAAANAER (1553.669) | |||||
| 8 | Snake venom metalloproteinase ACLF | VM1A_AGKCL | Agkistrodon piscivorus loucostroma | 47.1 | 67 | YVELVIIADHR (1327.857) |
| 29 | SHDNAQLLATAIVFDGIIGR (2169.126) | |||||
| VM1A_AGKCL | Agkistrodon contortrix latiematus | 26.7 | 77 | YVELVIVADHR (1313.725 ) | ||
| Zinc metalloproteinase disintegrin | VM2AB_AGKCO | Agkistordon contortrix contortrix | 55.1 | 185 | ISHDNAQLLTAIELDGETIGLANR (2564.272 ) | |
| 41 | YIELVVVADHR (1313, 713) | |||||
| Snake venom metalloproteinase VMP1 | VM1V1_AGKPL | Agkistrodon piscivorus leucostoma | 47.1 | 136 | SHDNAQLLTAIVFDEGIIGR (2169.058) | |
| 37 | APLAGMCDPNR (1201.591) | |||||
| 43 | YVELVIVADHR (1327.784) | |||||
| Zinc metalloproteinase disintegrin-like HR1a | VM3HA_PROFL | Protobothrops flavoviridis | 70.9 | 59 | TWVYEIVNTLNEIYR (1912.993) | |
| Snake venom metalloproteinase fibrolase | VM1F_AGKCO | Akgistrodon contortrix contortrix | 23.2 | 42 | YVQLVIVADHR (1312.613) | |
| 9 | Acidic phospholipase A2 BpirPLA2-I | PA2A1_BOTPI | Bothrops pirajai | 14.4 | 48 | CCFVMDCCYGK (1505.585) |
| 49 | QICECDR (980.433) | |||||
| Acidic phospholipase A2 S1E6-b | PA2AB_CALRH | Calloselasma rhodostoma | 14.3 | 56 | PMF SC 30.2% | |
| Acidic phospholipase A2 | PA2A_GLOHA | Gloydius halys | 14.7 | 57 | PMF SC 25.8 % | |
| Acidic phospholipase A2 1 | PA2A1_PROFL | Protobothrops flavoviridis | 15.5 | 30 | AAAICFR (808.334) | |
| 10 | C-type lectin APL | LECG_AGKPI | Agkistrodon piscivorus piscivorus | 16.7 | 103 | PMF SC 51.1% |
| 54 | DFSWEWTDR (1241.611) | |||||
| 105 | EFCVELVSLTGYR (1572.785) | |||||
| 101 | GQAEVWIGLWDK (1401.639) | |||||
| C- type lectin PAL | LECG_BITAR | Bitis arietans | 16.6 | 56 | PMF SC 58.5% |
# Spot numbering was the same as in Figure 1 and Figure 2; & Protein name in database; * Database accession number of homologous proteins; ¥ Organism from which protein identification originates; £ The mass of molecule; ± Protein identification was performed using the Mascot search with probability based Mowse score. Ions score was −10 × log(P), where P was the probability that the observed match was a random event. Mascot defined thresholds which indicated identity or extensive homology (p < 0.05) was 26; ¤ Peptide sequence derived from LIFT analysis. Identification of proteins by MS/MS method was conducted by comparing obtained sequences with sequences from database. In brackets: mass of precursor ion. In the case of PMF identification SC—amino acid sequence coverage for the identified proteins. In the PMF identification case the highest score and SC shown. Representative MS and MS/MS spectra used for the protein identification are included as supplementary material.