Biochemical and hemostatic description of a thrombin-like enzyme TLBro from Bothrops roedingeri snake venom.

ABSTRACT: Objective: The current study's objective is to characterize a new throm-bin-like enzyme called TLBro that was obtained from Bothrops roedingeris snake from a biochemical and hemostatic perspective. Methodology: One chromatographic step was used to purify it, producing the serine protease TLBro. Molecular mass was estimated by SDS-PAGE to be between reduced and unreduced by 35 kDa. Tryptic peptide sequencing using Swiss Prot provided the complete amino acid sequence. Expasy.org by conducting a search that is limited to Crotalinae snake serine proteases and displaying a high degree of amino acid sequence. Results: Ser (182) is inhibited by phenylmethylsulfonyl fluoride (PMSF), and TLBro demonstrated the presence of Asp (88) residues. It also deduced the positions

SUBMITTER: Vilca-Quispe A 

PROVIDER: S-EPMC10720248 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature