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Toxins 2017, 9(11), 373;

Comparative Study of Biological Activities of Venom from Colubrid Snakes Rhabdophis tigrinus (Yamakagashi) and Rhabdophis lateralis

Department of Microbiology, Faculty of Pharmacy, Meijo University, 150 Yagotoyama, Tenpaku-ku, Nagoya 468-8503, Japan
Emergency Medical Center, Kagawa University Hospital, 1750-1 Ikenobe, Miki, Kita, Kagawa 761-0793, Japan
Department of Biosafety, National Institute of Infectious Disease, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan
The Japan Snake Institute, Yabuzuka 3318, Ota, Gunma 379-2301, Japan
Department of Immunology, National Institute of Infectious Disease, Toyama 1-23-1, Shinjuku, Tokyo 162-8640, Japan
Department of Medical Entomology, National Institute of Infectious Disease, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan
Author to whom correspondence should be addressed.
Academic Editor: Frank S. Markland
Received: 23 August 2017 / Revised: 14 November 2017 / Accepted: 15 November 2017 / Published: 17 November 2017
(This article belongs to the Section Animal Venoms)
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Rhabdophis lateralis, a colubrid snake distributed throughout the continent of Asia, has recently undergone taxonomic revisions. Previously, Rhabdophis lateralis was classified as a subspecies of R. tigrinus (Yamakagashi) until 2012, when several genetic differences were discovered which classified this snake as its own species. To elucidate the toxicity of venom from this poorly studied colubrid, various biological activities were compared between the venom from the two snake species. The components of their venom were compared by the elution profiles of reversed-phase HPLC and SDS-PAGE, and gel filtrated fractions were tested for effects on blood coagulation. Proteolytic activities of these fractions were also assayed by using synthetic substrates, fibrinogen, and matrix proteins. Similar to the R. tigrinus venom, the higher molecular weight fraction of R. lateralis venom contained a prothrombin activator. Both prothrombin time (PT) and activated partial thromboplastin time (APTT) of human plasma were shortened by the addition of R. lateralis and R. tigrinus venom. The thrombin formation was estimated by the uses of SDS-PAGE and chromogenic substrates. These venom fractions also possessed very specific proteinase activity on human fibrinogen, but the substrates for matrix metalloproteinase, such as collagen and laminin, were not hydrolyzed. However, there were some notable differences in reactivity to synthetic substrates for matrix metalloproteinase, and R. tigrinus venom possessed relatively higher activity. Our chemical investigation indicates that the components included in both venoms resemble each other closely. However, the ratio of components and proteolytic activity of some ingredients are slightly different, indicating differences between two closely-related snakes. View Full-Text
Keywords: Rhabdophis tigrinus; Rhabdophis lateralis; snake venom; prothrombin activator; blood coagulation Rhabdophis tigrinus; Rhabdophis lateralis; snake venom; prothrombin activator; blood coagulation

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Komori, Y.; Hifumi, T.; Yamamoto, A.; Sakai, A.; Ato, M.; Sawabe, K.; Nikai, T. Comparative Study of Biological Activities of Venom from Colubrid Snakes Rhabdophis tigrinus (Yamakagashi) and Rhabdophis lateralis. Toxins 2017, 9, 373.

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