The absence of thrombin-like activity in Bothrops erythromelas venom is due to the deletion of the snake venom thrombin-like enzyme gene
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Purification and Partial Characterization of a Thrombin-Like Enzyme (AH144) from Venom of Iranian Snake Agkistrodon Halys
The snake venom´s thrombin-like enzymes comprise a number of serine proteases, which are functionally and structurally related to thrombin. Purification and partial characterization of a thrombin-like enzyme from the venom of the Iranian snake, Agkistrodon halys, was the aim of this study. Purification was carried out by a combination of variety of chromatographic methods that included: gel...
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The thrombin-like activities from the snake venoms of two subspecies of Bothrops atrox, moojeni (type I) and marajoensis (type II), were purified to homogeneity by affinity chromatography on a support consisting of the inhibitor, p-aminobenzamidine, linked to Sepharose 4B with a spacer of diaminodipropylaminosuccinate. At room temperature the enzyme was not bound to the affinity support but rat...
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Gabonase, an enzyme which acts on fibrinogen and factor XI11 in uniquely thrombin-like ways, was purified to electrophoretic homogeneity from the venom of Bitis gabonica. On sodium dodecyl sulfate-polyacrylamide electrophoresis, the reduced protein behaved as a single chain with Mr = 30,600. The enzyme contains 20.6% carbohydrate, no free sulfhydryl groups and hence, from amino acid analysis, f...
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A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose and ion-exchange chromatography on DEAE-Sepharose. The enzyme accounts for approximately 0.13% of the venom dry weight and has a molecular mass of 32 kDa as determined by SD...
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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 spectrometr...
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ژورنال
عنوان ژورنال: PLOS ONE
سال: 2021
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0248901