Snake Venom Proteases Affecting Blood Coagulation and Fibrinolysis

Stocker, Kurt

doi:10.1016/b978-0-08-024952-0.50017-x

Cited by 15 publications

(13 citation statements)

References 26 publications

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“…2, lane 2). The N-linked carbohydrate content calculated for afalcytin chains a and P is high but comparable with those reported for several other thrombin-like proteinases, including those from snake venom such as okinaxobin (18-19%, Iwasaki et al, 1990), ancrod (29 %, Kornalik, 1991, batroxobin (27 %, Stocker, 1990) and gabonase (20.6%, Pirkle et al, 1986). The sugar moieties did not appear to be involved in the catalytic activity of afalcytin.…”

Section: Discussionsupporting

confidence: 51%

“…This is the case for ancrod (Kornalik, 1991), batroxobin (Stocker, 1990), flavoxobin (Shieh et al, 1988) and proteinase RP34, which only forms fibrin monomers (Laraba-Djebari et al, 1992, and unpublished results). Other venom proteinases split both the Aa and then the BP chains of fibrinogen, thus allowing fibrin polymers to form; this is the case for crotalase, gabonase and cerastobin which, like thrombin (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Afaâcytin, an αβ‐fibrinogenase from Cerastes cerastes (Horned Viper) Venom, Activates Purified Factor X and Induces Serotonin Release from Human Blood Platelets

Laraba-Djebari

Martin‐Eauclaire

Mauco

et al. 1995

European Journal of Biochemistry

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Afalcytin, a proteinase with caseinolytic, arginine-esterase and amidase activities, was purified from the venom of Cprustes cerustes (horned viper) in two steps by gel filtration through Sephadex '375, then HPLC on carboxymethyl-cellulose. AfaBcytin has an isoelectric point of 6.25. and consists of two subunits, m and /], which have the same apparent molecular mass (40000) and are indistinguishable in the absence of reduction orkand deglycosylation. Subunit /) is constituted of two disulfide-linked polypeptidic chains, , O and f . The respective apparent molecular inass of the chains are 43000 (u), 35500 (/)) and 10200 (p') as determined by SDS/PAGE under reducing conditions. Both chains a and / l are N-glycosylated. The two chains have the same N-terminal sequence (20 residues) which is similar to those of other proteinases from snake venom. Susceptibility of afalcytin to diisopropyl fluorophosphate and benzamidine indicates the presence of a serine and an aspartic (or glutamic) acid residues in the catalytic site.Ca'+ appears to be required for structural cohesion of the afaBcytin molecule. Afalcytin exhibits apfibrinogenase and rx-fibrinase properties. It replaces missing factors VIII and IX in deficient plasmas, and activates purified human factor X into factor Xa. It releases serotonin from platelets and directly aggregates human (but not rabbit) blood platelets. Despite its thrombin-like characteristics, however, afalcytin is not inhibited by plasmatic thrombin inhibitors. The procoagulant properties of afalcytin therefore have potential clinical applications.

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Section: Discussionsupporting

confidence: 51%

Section: Discussionmentioning

confidence: 99%

Afaâcytin, an αβ‐fibrinogenase from Cerastes cerastes (Horned Viper) Venom, Activates Purified Factor X and Induces Serotonin Release from Human Blood Platelets

Laraba-Djebari

Martin‐Eauclaire

Mauco

et al. 1995

European Journal of Biochemistry

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“…At predetermined time intervals (5 min, 0.5 h, 20 h), the reaction mixture (25 Ìl) was frozen to stop the reaction. Before MALDI-TOF analysis, samples were purified from salts using ZipTip C 4 or ZipTip C 18 according to Millipore instructions. The matrix used for human factor X, VLFXA and cleavage products of factor X was ferulic acid, cytochrome C was used for mass calibration.…”

Section: Maldi-tof Msmentioning

confidence: 99%

Proteases from <i>Vipera lebetina </i>Venom Affecting Coagulation and Fibrinolysis

Siigur¹,

Aaspõllu²,

Tõnismägi³

et al. 2001

Pathophysiol Haemos Thromb

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Our studies of the venom from the Levantine viper Vipera lebetina have demonstrated the existence of both coagulants and anticoagulants in the same venom. We showed that V. lebetina venom contains: (1) proteases that degrade fibrinogen, but not fibrin; (2) fibrinolytic enzyme (lebetase); (3) factor X activator (VLFXA); (4) factor V activator (VLFVA). Fibrinolytic enzyme and VLFXA are metalloproteases; the other studied enzymes are serine proteases. α-Fibrinogenase has no homolog among known serine proteases. β-Fibrinogenase is a typical thermostable arginine esterase that hydrolyzes esters and amides of arginine and attacks the β-chain of fibrinogen. Lebetase is a direct-acting fibrinolytic zinc metalloendopeptidase related in amino acid sequence to reprolysins. We used the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry technique for the recovery and identification of peptides released by protease hydrolysis and for the detection of human factor X cleavage products after VLFXA hydrolysis. VLFXA cleaves the Arg⁵²-Ile⁵³bond in the heavy chain of human factor X and the Arg²²⁶-Val²²⁷ bond in human factor IX precursor; VLFVA cleaves Arg¹⁵⁴⁵-Ser¹⁵⁴⁶ in factor V.

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“…Snake venoms are complex mixtures, which contain many enzymes and inhibitors involved in blood coagulation or platelet aggregation (Stocker, 1990). These proteins can be classified into several categories depending on their hemostatic action.…”

Section: Introductionmentioning

confidence: 99%

Affinity-purification of fibrinogenase with high proteolytic activity from Agkistrodon halys (Chinese) Venom

Zhang²,

Wu³

et al. 2008

Arch. Pharm. Res.

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To purify and characterize the fibrinogenase with high proteolytic activity from Agkistrodon halys (Chinese) Venom. Monoclonal antibodies against fibrinogenase were prepared and a novel affinity chromatography equipped with a monoclonal antibody against fibrinogenase was developed and applied for the purification of fibrinogenases. The purified fibrinogenase was identified by fibrinolytic activity assay, and antithrombosis activity assay. HPLC chromatography and SDS-PAGE analysis demonstrated the uniformity and purity of the purified fibrinogenase. In comparison with a conventional A-50 chromatography method, affinity-purified fibrinogenase showed higher activity (3631 U mg(-1) vs 501 U mg(-1)). In addition, the physiological activity of the fibrinogenase both in vitro and ex vivo showed the purified fibrinogenase can specifically degrade beta-, gamma-fibrinogen and has a high anti-thrombotic activity. In conclusion, the purified fibrinogenase by affinity column were shown to be homogeneous and showed a high and specific proteolytic activity against beta-chains of fibrinogen molecules and antithrombosis activity.

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Snake Venom Proteases Affecting Blood Coagulation and Fibrinolysis

Cited by 15 publications

References 26 publications

Afaâcytin, an αβ‐fibrinogenase from Cerastes cerastes (Horned Viper) Venom, Activates Purified Factor X and Induces Serotonin Release from Human Blood Platelets

Afaâcytin, an αβ‐fibrinogenase from Cerastes cerastes (Horned Viper) Venom, Activates Purified Factor X and Induces Serotonin Release from Human Blood Platelets

Proteases from <i>Vipera lebetina </i>Venom Affecting Coagulation and Fibrinolysis

Affinity-purification of fibrinogenase with high proteolytic activity from Agkistrodon halys (Chinese) Venom

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