Biochemical properties and comparative pharmacology of a coagulant from Deinagkistrodon acutus snake venom

Tang, Song-Shan; Wang, Xiaohua; Zhang, Juan-Hui; Tang, Bo-Shan; Li, Qian; Li, Peiying; Luo, Lixia

doi:10.1016/j.ejps.2013.02.002

Cited by 16 publications

(8 citation statements)

References 9 publications

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“…Like the majority of serine proteases [12, 13, 20, 44–48], these differences indicate that BpirSP-39 seems to be a glycosylated protein. The difference detected during electrophoretic migration was probably caused by the carbohydrate microheterogeneity of the enzyme since this fraction can vary the weight of the serine protease up to 30%.…”

Section: Discussionmentioning

confidence: 97%

“…If BpirSP-39 acted indirectly, activating prothrombin, the resulting thrombin would be inactivated by heparin preventing fibrin network formation. In this same way, the clotting activity of Agacutase, a recent thrombin-like enzyme isolated from Deinagkistrodon acutus [12], was not influenced by heparin or hirudin, which is different from BjussuSP-I, a serineprotease from Bothrops jararacussu whose clotting ability was reduced by heparin [48]. …”

Section: Discussionmentioning

confidence: 99%

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Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Zaqueo

Kayano

Simões-Silva

et al. 2014

BioMed Research International

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This paper presents a novel serine protease (SP) isolated from Bothrops pirajai, a venomous snake found solely in Brazil that belongs to the Viperidae family. The identified SP, named BpirSP-39, was isolated by three chromatographic steps (size exclusion, bioaffinity, and reverse phase chromatographies). The molecular mass of BpirSP-39 was estimated by SDS-PAGE and confirmed by mass spectrometry (39,408.32 Da). The protein was able to form fibrin networks, which was not observed in the presence of serine protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF). Furthermore, BpirSP-39 presented considerable thermal stability and was apparently able to activate factor XIII of the blood coagulation cascade, unlike most serine proteases. BpirSP-39 was capable of hydrolyzing different chromogenic substrates tested (S-2222, S-2302, and S-2238) while Cu2+ significantly diminished BspirSP-39 activity on the three tested substrates. The enzyme promoted platelet aggregation and also exhibited fibrinogenolytic, fibrinolytic, gelatinolytic, and amidolytic activities. The multiple alignment showed high sequence similarity to other thrombin-like enzymes from snake venoms. These results allow us to conclude that a new SP was isolated from Bothrops pirajai snake venom.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Zaqueo

Kayano

Simões-Silva

et al. 2014

BioMed Research International

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“…Among them, medicinal animals are a major source of thrombolytic agents, such as lumbrokinase and earthworm fibrinolytic enzyme II from earthworms [8,33], Agacutase from D. acutus snake venoms [10,11], hirudins from leech Hirudinaria manillensis [6], fibrinolytic protease UFEIII from Urechis unicinctus [4], and several of these compounds, such as hirudin [34], lumbrokinase [35], ancrod [36] have been widely applied in the clinic and achieved good results.…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Tian

Лі

Li-wei

et al. 2015

International Journal of Biological Macromolecules

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“…Direct fibrino(geno)lysis (Wang et al, 2004) and partly consumptive coagulopathy participated in this process. Consumption cascade can be induced by prothrombin activators and/or directly acting non-inhibited thrombin isoenzymes in snake venom (Tang et al, 2009(Tang et al, , 2013. Stationary antithrombin (AT) levels indicate the effect of thrombin-like isoenzymes which are non-inhibitable by AT.…”

Section: Discussionmentioning

confidence: 99%

Envenoming by Crotalid Snake Chinese Moccasin Agkistrodon Acutus Bite – A Case Report

2015

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Although the bites caused by snakes from former Agkistrodon family in the areas of occurrence are not rare and even have certain epidemiologic importance, in case of envenoming by Deinagkistrodon acutus the clinical studies and case reports are very sporadic. This case report describes the envenoming of a private snake breeder bitten by young Chinese moccasin Deinagkistrodon acutus to the thumb of his left hand. He sought for a medical help immediately after snakebite. Patient presented with a local oedema on the affected limb, extending up to the half of the forearm. Laboratory examinations showed serious haemostatic disturbance with defibrination syndrome, immeasurably prolonged clotting times and extreme elevation of D-dimers. No other obvious clinical symptoms were present. Fibrinogen and fresh frozen plasma were administered because the antivenom was not available immediately. The specific antivenom was urgently imported 22 hours after the bite and administered at a dose of two vials three times until laboratory haemocoagulation parameters returned back to physiological values.

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Biochemical properties and comparative pharmacology of a coagulant from Deinagkistrodon acutus snake venom

Cited by 16 publications

References 9 publications

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom

Purification and biochemical characterization of a novel fibrinolytic enzyme, PSLTro01, from a medicinal animal Porcellio scaber Latreille

Envenoming by Crotalid Snake Chinese Moccasin Agkistrodon Acutus Bite – A Case Report

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