Purification and Properties of a Thrombin-like Enzyme from the Venom of Crotalus adamanteus (Eastern Diamondback Rattlesnake)

Purification and properties of a thrombin-like enzyme from the venom of Crotalus adamanteus (Eastern diamondback rattlesnake).

The genetics of venom ontogeny in the eastern diamondback rattlesnake (Crotalus adamanteus)

The same selective forces that give rise to rapid inter- and intraspecific divergence in snake venoms can also favor differences in venoms across life-history stages. Ontogenetic changes in venom composition are well known and widespread in snakes but have not been investigated to the level of unambiguously identifying the specific loci involved. The eastern diamondback rattlesnake was previous...

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...

Wound Healing Activity and Mechanisms of Action of an Antibacterial Protein from the Venom of the Eastern Diamondback Rattlesnake (Crotalus adamanteus)

Basic phospholipase A2 was identified from the venom of the eastern diamondback rattlesnake. The Crotalus adamanteus toxin-II (CaTx-II) induced bactericidal effects (7.8 µg/ml) on Staphylococcus aureus, while on Burkholderia pseudomallei (KHW), and Enterobacter aerogenes were killed at 15.6 µg/ml. CaTx-II caused pore formation and membrane damaging effects on the bacterial cell wall. CaTx-II wa...

Purification and Some Properties of Two Proteinases from Crotalus adamanteus Venom That Inactivate Human al-Proteinase

Two proteinases (proteinases I and II) have been purified from Crotalus adamanteus venom to the stage of electrophoretic homogeneity and proteinase II has been crystallized. The proteinases differ slightly in molecular weight and amino acid composition. Both are metalloenzymes requiring Zn2+ or Ca2+, or both; neither requires thiol compounds for activation. The proteinases are free of esterolyt...