Biochemical and Hemostatic Mechanism of A Novel Thrombin-Like Enzyme

Tang, Song-Shan; Zhang, Juan-Hui; Tang, Bai-Shan; Tang, Zhihua; Li, Hongzhi; Yuan, Hao-Jia; Chui, Shu-Lian; Zhao, Er-Yao

doi:10.1016/j.thromres.2009.06.022

Cited by 13 publications

(8 citation statements)

References 11 publications

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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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Section: Discussionmentioning

confidence: 99%

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

2015

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“…Most SVTLEs are serine-proteases (Sant' Ana et al, 2008;Tang et al, 2009;Costa Jde et al, 2010). Malabarin, a metalloprotease, is an exception (Gowda et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Kumar

Manjunath

Joshi

et al. 2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…Snake venom serine proteases belong to trypsin S1 family clan SA. To date, a large number of studies, including molecular cloning, have led to the isolation and identification of TLEs mainly from the venom of subfamily Viperinaeand Crotalinae [3][4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity fromBothrops barnettiSnake Venom

et al. 2013

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A thrombin-like enzyme named TLBbar was isolated from Bothrops barnetti snake venom and its biochemical and pharmacological characteristics were determined. TLBbar was purified using size exclusion chromatography and reverse phase HPLC, showing molecular mass of 28750.7 Da determined by mass spectrometry. TLBbar serine protease is basic (pI 7.4) and its structure shows similarity with other serine proteases of snake venom. Optimal proteolytic activity was at 37 ∘ C and pH 8; this activity was strongly inhibited by PMSF and Leupeptin, however; heparin, and soybean trypsin inhibitor (SBT-I) were ineffective. Kinetic studies on BApNA chromogenic substrate have revealed that TLBbar presents a Michaelis-Menten kinetics, with values of and max of 0.433 mM and 0.42 nmol/min, respectively. TLBbar showed high clotting activity upon bovine and human plasma, presenting IC of 125 and minimum dose coagulant (MDC) of 2.23 g/ L. TLBbar cleavages the A chain of bovine fibrinogen, with maximal efficiency at 30-40 ∘ C in the presence of calcium after two hours incubation; this fibronogenolityc activity was inhibited by PMSF and Leupeptin, confirming its classification in the group of serine proteases. In addition, TLBbar is capable of aggregating platelets in the same way that thrombin in concentrations of 2.5 g/ L.

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Biochemical and Hemostatic Mechanism of A Novel Thrombin-Like Enzyme

Cited by 13 publications

References 11 publications

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

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

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity fromBothrops barnettiSnake Venom

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