PaperPurification and characterization of platelet aggregation inhibitors from snake venoms
References (25)
- et al.
Trigramin, a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex
J. Biol. Chem.
(1987) - et al.
Echistatin, a potent platelet aggregation inhibitor from the viper, Echis carinatus
J. Biol. Chem.
(1988) - et al.
Elegantin and Alborabin purified peptides from viper venoms; homologies with the RGDS domain of fibrinogen and von Willebrand factor
Biochim. Biophys. Acta
(1990) - et al.
Barbourin, a GPIIb/IIIa specific antagonist from the venom of Sisturus m. barbouri
J. Biol. Chem.
(1991) - et al.
Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms
J. Biol. Chem.
(1993) - et al.
Measurement of protein using bicinchoninic acid
Anal. Biochem.
(1985) - et al.
Tricine-SDS PAGE for the seperation of proteins in the range of 1 to 100 kDa
Anal. Biochem.
(1987) - et al.
Antithrombotic properties of L-cysteine, N-(mercaptoacetyl)-D-Tyr-Arg-Gly-Asp-sulfoxide (G4120) in a hamster platelet-rich femoral vein thrombosis model
Blood
(1992) - et al.
Design of potent and specific integrin antagonists
- et al.
Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
Toxicon
(1992)
Cited by (71)
Preclinical studies of a novel snake venom-derived recombinant disintegrin with antitumor activity: A review
2020, Biochemical PharmacologyCitation Excerpt :Many of them were characterized structurally and functionally and were confirmed to interact with and inhibit specific integrins, generating further efforts to study their potential anticancer activities. In our own studies, the Markland lab discovered contortrostatin (CN) in 1994 [41,42] a homodimeric disintegrin from the venom of Agkistrodon contortrix contortrix, the Southern copperhead snake (Fig. 1). CN has become one of the most-studied members of this group of snake venom disintegrins.
Development of a chimeric recombinant disintegrin as a cost-effective anti-cancer agent with promising translational potential
2012, ToxiconCitation Excerpt :When proteolysis was complete, the proteolyzed lysates were passed through a 0.22 μm filter, diluted 1:100 in ddH2O, ultrafiltrated through a 50,000 MWCO cartridge (Biomax50, Millipore) and then reconcentrated against a 5000 MWCO cartridge (Biomax5, Millipore) using a tangential flow ultrafiltration device (Labscale TFF system, Millipore). Purification was accomplished by C-18 reverse phase HPLC using the standard elution conditions previously employed for the purification of native CN (Trikha et al., 1994b). The filtrated lysates processed as described above were loaded onto a Vydac C-18 column (218TP54, Temecula, CA).
Biochemistry of Envenomation
2012, Advances in Clinical Chemistry