Purification and characterization of patagonfibrase, a metalloproteinase showing α-fibrinogenolytic and hemorrhagic activities, from Philodryas patagoniensis snake venom

Peichoto, María Elisa; Teibler, Pamela; Mackessy, Stephen P.; Leiva, Laura; Acosta, Ofelia; Gonçalves, L.R.C.; Tanaka-Azevedo, Anita Mitico; Santoro, Marcelo Larami

doi:10.1016/j.bbagen.2006.12.014

Cited by 74 publications

(71 citation statements)

References 49 publications

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“…Venoms of Colubridae snakes are a rich source of novel compounds that may have applications in medicine and biochemistry (16). This article reports a relatively simple procedure for the isolation of an anticoagulant factor from Iranian Agkistrodon halys venom, denominated AH22, which was isolated and purified by a combination of gel filtration on Sephadex G-50 ( Figure 1) and ion-exchange chromatography on DEAESepharose ( Figure 2).…”

Section: Discussionmentioning

confidence: 99%

“…By this procedure the total enzyme purification yield was about 83% (Table 1), thus enabling the conclusion that the protocol utilized was highly efficient. Fractionation and purification of snake venom constituents have been carried out through several chromatography methods (6)(7)(8)16). An acidic As described in the Introduction section, snake venom toxins that prolong blood coagulation are proteins or glycoproteins that inhibit blood coagulation by different mechanisms.…”

Section: Discussionmentioning

confidence: 99%

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Identification and partial purification of an anticoagulant factor from the venom of the Iranian snake Agkistrodon halys

Ghorbanpur¹,

Mirakabadi²,

Zokaee³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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An anticoagulant factor was purified from the venom of the Iranian snake Agkistrodon halys by gel filtration on Sephadex G-50 and ion-exchange chromatography on DEAE-Sepharose. In the final stage of purification, the percentage recovery of purified anticoagulant factor was found to be 83%. The purified anticoagulant factor revealed a single protein band in SDS-polyacrylamide electrophoresis under reducing conditions and its molecular weight was about 22 kDa. The purified peptide did not show any effect on casein, BApNA or plasma.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification and partial purification of an anticoagulant factor from the venom of the Iranian snake Agkistrodon halys

Ghorbanpur¹,

Mirakabadi²,

Zokaee³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Such modifications are caused by the binding of zinc to non-catalytic ion-binding sites, resulting in a conformation change that leads to the loss of proteolytic activity (Zhu et al, 1997;Peichoto et al, 2007). Other cations, Fe 3+ , Mn 2+ , Ni 2+ , Co 2+ , Cu 2+ and Hg 2+ acted as inhibitors, whereas Al 3+ has no effect on the enzymes activity (Table 3).…”

Section: Characterization Of the Isolated Proteolytic Enzymesmentioning

confidence: 99%

“…Although the hemorrhagic SVMPs are zinc-dependent, the inhibition of protease activity of purified SVMPs by adding Zn 2+ was not surprising, since other SVMPs were also inactivated by treatment with zinc (Peichoto et al, 2007). Such modifications are caused by the binding of zinc to non-catalytic ion-binding sites, resulting in a conformation change that leads to the loss of proteolytic activity (Zhu et al, 1997;Peichoto et al, 2007).…”

Section: Characterization Of the Isolated Proteolytic Enzymesmentioning

confidence: 99%

Purification and characterization of five snake venom metalloproteinases from Egyptian <i>Echis pyramidum </i><i>pyramidum</i> venom

Abdel‐Aty¹,

Wahby²

2014

J. Toxicol. Sci.

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-New five P-III snake venom metalloproteinases (SVMPs): EpyB2 (62 kDa), EpyB3 (62+23 kDa), EpyB4 (60 kDa), EpyB5 (67 kDa) and EpyB6 (66 kDa) of the most dangerous viper, Echis pyramidum pyramidum (Epy), were purified and characterized in a set of biochemical assays. The SVMPs were purified by applying a protocol of two successive chromatographic steps. Three purified SVMPs "EpyB2, EpyB4, and EpyB5" have hemorrhagic activity with MHDs, 7 μg, 7.6 μg and 15 μg, respectively; furthermore, they have high preference towards fibronectin, collagen, gelatin, fibrin and hemoglobin substrates compared with non-hemorrhagic SVMPs (EpyB3 and EpyB6). All the purified SVMPs showed remarkable thermal and pH stability, inhibited by metalloproteinase inhibitors and Zn 2+ , Mn 2+ , Ni 2+ , Co 2+ , Cu 2+ , and Hg 2+ . The purified SVMPs act as α-fibrinogenases, prothrombin activators and procoagulants. In conclusion, Epy venom has multiple SVMPs that are responsible for hemorrhagic events and thus represent a significant health hazard for victims of envenomation, however, they may be useful for treating diseases involving abnormal blood clot formation.

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“…While enzymes are present in the majority of venoms [18][19][20][21][22][23][24][25][26][27][28], their number in invertebrates is very limited compared to that in snake venoms. As ArachnoServer and ConoServer deal with invertebrate proteins, data on enzymes are either limited, or nonexistent.…”

Section: Enzymesmentioning

confidence: 99%

Animal Toxins: How is Complexity Represented in Databases?

Jungo¹,

Estreicher

Bairoch

et al. 2010

Toxins

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Peptide toxins synthesized by venomous animals have been extensively studied in the last decades. To be useful to the scientific community, this knowledge has been stored, annotated and made easy to retrieve by several databases. The aim of this article is to present what type of information users can access from each database. ArachnoServer and ConoServer focus on spider toxins and cone snail toxins, respectively. UniProtKB, a generalist protein knowledgebase, has an animal toxin-dedicated annotation program that includes toxins from all venomous animals. Finally, the ATDB metadatabase compiles data and annotations from other databases and provides toxin ontology.

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Purification and characterization of patagonfibrase, a metalloproteinase showing α-fibrinogenolytic and hemorrhagic activities, from Philodryas patagoniensis snake venom

Cited by 74 publications

References 49 publications

Identification and partial purification of an anticoagulant factor from the venom of the Iranian snake Agkistrodon halys

Identification and partial purification of an anticoagulant factor from the venom of the Iranian snake Agkistrodon halys

Purification and characterization of five snake venom metalloproteinases from Egyptian <i>Echis pyramidum </i><i>pyramidum</i> venom

Animal Toxins: How is Complexity Represented in Databases?

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