Research Article

Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis muta rhombeata Snake Venom

Figure 4

The amino acid sequence alignment of Rhombeobin with selected serine proteases sequences obtained from the BLAST protein data bank (PubMed/Medline). LM-TL, Lachesis muta muta [11]; gyroxin, Crotalus durissus terrificus [12]; bilineobin, Agkistrodon bilineatus [13]; bothrombin, Bothrops jararaca [14]; bjussuSP-I, B. jararacusu [15]; batroxobin, B. atrox [16]; acutobin, Agkistrodon acutus [17]; ancrod, Agkistrodon rhodostoma [18]. Numbering is according to ANCROD. Catalytic triad residues are shown in grey, and conserved cysteinve residues are shown by “*”. Specificity sites and the residues forming the hydrophobic site are shown by “+” and “”, respectively, according to Castro et al. [19].
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