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Elegantin and angustatin, which were isolated from the snake venoms of Protobothrops elegans and Dendroaspis angusticeps, markedly inhibit binding between platelet integrins and fibrinogen via the Arg-Gly-Asp (RGD) sequence. Angustatin, which is a three-finger toxin containing the RGD sequence, inhibits platelet aggregation almost ten times more strongly than disintegrin isolated from the venoms of...
We herein identified two high molecular mass metalloproteinases, named SV-PAD-2 and HR-Ele-1, in the venom of Protobothrops elegans. HR-Ele-1 appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) regard under reducing and non-reducing conditions, and the molecular mass of this protease was approximately 60 kDa under reducing conditions. On the other hand,...
A low molecular weight metalloproteinase, named PT-H 2 protease, with fibrinolytic activity, was purified from the venom of Protobothrops tokarensis (Tokara-habu) by gel-filtration using Sephadex G-100, and ion-exchange chromatographies using CM-Sepharose Fast Flow and Mono S HR 5/5. By this procedure, about 85 mg of purified protein were obtained from 1.0 g of P. tokarensis venom. The purified...
A platelet aggregation inhibitor, named snake venom platelet aggregation dissociator (SV-PAD)-1, with a dissociative reaction of ADP-induced platelet aggregation, was purified from the venom of Protobothrops elegans (Sakishima-habu) by gel-filtration employing Sephadex G-100, and ion-exchange chromatographies using DEAE-Sepharose Fast Flow, CM-Sepharose Fast Flow, and Mono S. By this procedure, about...
The amino acid sequence of a bradykinin-releasing enzyme, named KR-E-1, isolated from the venom of Agkistrodon caliginosus (Kankoku-mamushi) was determined by Edman sequencing of the peptides which was derived from digests with cyanogen bromide, hydroxylamine, achromobacter protease I, trypsin, V8 protease, arginine endopeptidase, and endoproteinase Asp-N. KR-E-1 consisted of 235 amino acids and showed...
An assay of platelet aggregation inhibitors measured by the turbidimeter using Aggregometer PAM 8C (Mebanix) was performed after each crude snake venom (57 species) was subjected to ultrafiltration using MILLIPORE UFP 1 LGC. The snake venoms of Viperidae (three species), Elapidae (11 species), and Hydrophiidae (two species) inhibited ADP-induced rabbit platelet aggregation. In particular, six venoms...
We reported previously that elegaxobin and elegaxobin II cause the release of fibrinopeptide A alone from rabbit fibrinogen. Elegaxobin II is a thrombin-like enzyme that possesses kinin-releasing activity, and shows a characterization obviously different from elegaxobin. To study the substrate specificities of elegaxobin and elegaxobin II against fibrinogen, we investigated whether anti-elegaxobin...
The amino acid sequence of a thrombin like enzyme , named elegaxobin II, isolated from the venom of Trimeresurus elegans (Sakishima-habu) was determined by Edman sequencing of the peptides which was derived from digests with cyanogen bromide, achromobacter protease I, trypsin, endoproteinase Asp-N, and chymotrypsin. Elegaxobin II consisted of 233 amino acids and showed conservation of the catalytic...
A thrombin like enzyme, named elegaxobin II, with Lys-bradykinin releasing activity was purified from the venom of Trimeresurus elegans (Sakishima-habu) by gel-filtration on Sephadex G-100, and ion-exchange chromatography on the Q-Sepharose Fast Flow. By this procedure, about 9mg of purified enzyme was obtained from 1.1g of the venom. The purified enzyme showed a single protein band, the molecular...
The amino acid sequence of a thrombin like enzyme, named elegaxobin, isolated from the venom of Trimeresurus elegans (Sakishima-habu) was determined by Edman sequencing of the peptides, derived from digests with cyanogen bromide, hydroxylamine, achromobacter protease I, trypsin, V8 protease, and chymotrypsin. Elegaxobin showed conservation of the catalytic amino acid residues (His, Asp, and Ser) of...
A thrombin-like enzyme, named elegaxobin, was purified from the venom of Trimeresurus elegans (Sakishima-habu) by gel filtration on Sephadex G-100, and ion-exchange chromatographies on Q-Sepharose Fast Flow and S-Sepharose Fast Flow. By this procedure, about 8.5 mg of purified enzyme was obtained from 1.1 g of the venom. The purified enzyme showed a single protein band in SDS-polyacrylamide electrophoresis...
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