Animal experiments are challenging to carry out from a point of view in the prevention of cruelty to animals, this process may well grow to be pretty helpful for studying hemorrhage in the future. It truly is necessary to establish a method of cytotoxicity study using various hemorrhagic or non-hemorrhagic SVMPs. Author Contributions Yumiko Komori was responsible for experimental style, amino acid analysis, toxicity test on cells and writing the manuscript; Eri Murakami for purification of protein and digested peptides, enzymeToxins 2014,assays, hemorrhagic assays and gel electrophoresis experiments; Kei-ichi Uchiya for MALDI-TOF mass spectrometry; Tunemasa Nonogaki for histopathological experiment; and Toshiaki Nikai for experimental design and writing the manuscript. Conflicts of Interest The authors declare no conflict of interest. References Tu, A.T. Rattlesnake Venom: Their Actions and Therapy, 1st ed.; Marcel Dekker Inc.: New York, NY, USA, 1982. two. Shannon, J.D.; Baramova, E.N.; Bjarnason, J.B.; Fox, J.W. Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin. J. Biol. Chem. 1989, 264, 115751583. three. Takeya, H.; Onikura, A.; Nikai, T.; Sugihara, H.Pristinamycin ; Iwanaga, S. Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber. J. Biochem. 1990, 108, 71119. 4. Gong, W.; Zhu, X.; Liu, S.; Teng, M.; Niu, L. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase in the snake venom of Agkistrodon acutus. J. Mol. Biol. 1998, 283, 65768. five. Nikai, T.; Mori, N.; Kishida, M.; Sugihara, H.; Tu, A.T. Isolation and biochemical characterization of hemorrhagic toxin f from the venom of Crotalus atrox (western diamondback rattlesnake). Arch. Biochem. Biophys. 1984, 231, 30919. 6. Nikai, T.; Taniguchi, K.; Komori, Y.; Masuda, K.; Fox, J.W.; Sugihara, H. Key structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch. Biochem. Biophys. 2000, 378, 65. 7. Fox, J.W.; Bjarnason, J.B. Atrolysins: Metalloproteinases from Crotalus atrox venom. Approach. Enzymol. 1995, 248, 36887. 8. Omori-Satoh, T.; Sadahiro, S. Resolution of your significant hemorrhagic component of Trimeresurus flavoviridis venom into two parts. Biochim. Biophys. Acta 1979, 580, 39204. 9. Miyata, T.; Takeya, H.; Ozeki, Y.; Arakawa, M.; Tokunaga, F.; Iwanaga, S.; Omori-Satoh, T. Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis. J. Biochem. 1989, 105, 84753. 10. Masuda, S.; Hayashi, H.; Araki, S. Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin loved ones. Eur. J. Biochem.Temoporfin 1998, 253, 361.PMID:23937941 11. Fox, J.W.; Serrano, S.M. Structural considerations from the snake venom metalloproteinases, important members in the M12 reprolysin loved ones of metalloproteinases. Toxicon 2005, 45, 96985. 12. Hite, L.A.; Shannon, J.D.; Bjarnason, J.B.; Fox, J.W. Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: Proof for signal, zymogen, and disintegrin-like structures. Biochemistry 1992, 31, 6203211. 1.Toxins 2014,13. Shimokawa, K.; Shannon, J.D.; Jia, L.-G.; Fox, J.W. Sequence and biological activity of catrocollastatin-C: A disintegrin-like/cysteine-rich two-domain protein from Crotalus atrox venom. Arch. Biochem. Biophys. 1997, 343, 353. 14. White, J.M. ADAMs: Modulators.
