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Divergent and common groups of proteins in glands of venomous snakes
Author(s) -
Rioux Vincent,
Gerbod MarieChristine,
Bouet Françoise,
Ménez André,
Galat Andrzej
Publication year - 1998
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150190531
Subject(s) - zoology , biology , evolutionary biology , computational biology
Protein contents of venom‐producing glands from the sea‐snake Laticauda colubrina (LC) and terrestrial Vipera Russelli (VR) were studied using high‐resolution two‐dimensional gels: isoelectric focusing followed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (IEF/SDS‐PAGE) and nonequilibrium pH gradient electrophoresis (NEPHGE) followed by SDS‐PAGE. Tentative identities of numerous proteins were established using their amino acid compositions and in certain cases the identities were verified by microsequencing of their N ‐terminals and internal fragments. As expected, we found several proteins known to be present in the venom of the respective snakes. These include numerous isoforms of phospholipase A 2 (PLA 2 ) in both snake glands, various neurotoxins in LC glands and factor IX/factor X‐binding protein, hemorrhagic factor and coagulation factor X activating enzyme in Russell's viper glands (VR). Not unexpectedly, we also found a number of cell housekeeping proteins, cytoskeletal proteins, proteins that are necessary for folding, such as heat‐shock proteins, protein disulfide‐isomerase and peptidylprolyl cis/trans isomerases. Unexpectedly, however, the glands of Laticauda colubrina and Russell's viper include a large quantity of antihemmorhagic factor and inhibitor of PLA 2 , respectively, that have been previously described in snake plasma. The possible reason associated with the presence of these components in venom glands is discussed.