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Ol 1995, 10:7-12. 12. Lav -Murcio PA, Robinson BG, Kardong KV: Cues involved in relocation of struck prey by rattlesnakes, Crotalus viridis oreganus. Herpetologica 1993, 49:463-469. 13. Chiszar D, Hobika G, Smith HM, Vidaurri J: Envenomation and acquisition of chemical information by prairie rattlesnakes. Prairie Nat 1991, 23:69-72. 14. Hayes WK, Kaiser II, Duvall D: The mass of venom expended by prairie rattlesnakes when feeding on rodent prey. In Biology of the Pit Vipers. Edited by: Campbell JA, Brodie ED Jr. Tyler, TX: Selva Publishing; 1992:383-388. 15. Chiszar D, Lee RKK, Smith HM, Radcliffe CW: Searching behaviors by rattlesnakes following predatory strikes. In Biology of the Pit Vipers. Edited by: 6-Trichloronicotinic acid 8-Oxa-3-azabicyclo[3.2.1]octane hydrochloride 3-Hydroxyanthranilic acid PigmentRed179 4-CHLORO-2-NITROBENZALDEHYDE Diethyl 4-oxocyclohexane-1 Campbell JA, Brodie ED Jr. Tyler, TX: Selva Publishing; 1992:369-382. 16. Greenbaum E, Galeva N, Jorgensen M: Venom variation and chemoreception of the viperid Agkistrodon contortrix: evidence for adaptation? J Chem Ecol 2003, 28:1741-1755. 17. Chiszar D, Walters A, Smith HM: Rattlesnake preference for envenomated prey: species specificity. J Herpetol 2008, 42:764-767. 18. Chiszar D, Walters A, Urbaniak J, Smith HM, Mackessy SP: Discrimination between envenomated and nonenvenomated prey by western diamondback rattlesnakes (Crotalus atrox): chemosensory consequences of venom. Copeia 1999, 640-648. 19. Kardong KV, Kiene TL, Bels V: Evolution of trophic systems in squamates. Neth J Zool 1997, 47:411-427. 20. Fox JW, Serrano SMT: Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J 2008, 275:3016-3030.Samples of Peak III for sequencing were reduced with dithiothreitol and alkylated with iodoacetamide as described previously [48]. The first 30 resides of sequence were obtained PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/25386826 using an ABI Procise sequencer (Life Technologies/Applied Biosystems, Grand Island, NY, USA), and sequence obtained was subjected to Basic Local Alignment Search Tool (BLAST) at the National Center for Biotechnology Information (Bethesda, MD, USA) [49].Additional materialAdditional file 1: Table S1. Raw data: Number of 2-[(4S)-4,5-Dihydro-4-isopropyl-2-oxazolyl]pyridine tongue flicks toward 1-Methyl-3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-pyrazole envenomated (E) or non-envenomated (NE) mice. This table contains the raw data collected for behavioral experiments 1 and 2. Experiment 1 consisted of paired trials using a non-envenomated vs. and envenomated (whole venom) mouse – this trial was conducted to replicate and confirm past results. Experiment 2 consisted of the same paired trials, but instead of whole venom, one of five size exclusion venom fractions, Peak I, IIa IIb, III or Peptides, was used in “envenomated” mice. Trials were of 10 minutes duration, and the number of tongue flicks directed toward one or the other mouse was recorded. Additional file 2: Figure S1. Reducing SDS-PAGE analysis of size exclusion chromatography fractions. Ten micrograms of protein (reduced with DTT) from each size exclusion peak (BioGel P100) were loaded onto a 12 acrylamide NuPage gel. Following electrophoresis, the gel was fixed and stained with 0.1 Coomassie Brilliant Blue R250 using standard methods, destained and photographed. MW standards = Invitrogen Mark 12. Circled faint bands indicate carryover contamination of metalloproteinases (darkest bands) from lanes 2 and 4, respectively. Note that lane 5 is the only peak containing disintegrin bands (dark pair, red bracket); peptides PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/8833965 were not visualized and are smaller than the resolution capability of the gel.Abbreviatio.