Biochemical characterization of Walterinnesia morgani (desert black cobra) venom (Serpentes: Elapidae)

Abstract

Snake venom contains various bioactive proteins and peptides, of which enzymes make up a significant portion. Desert Black Cobra (Walterinnesia morgani) is a venomous snake distributed mainly in the Middle East including southeastern Türkiye. The aim of the present study is to investigate the key enzyme activities and protein profile of W. morgani venom originating from Sanliurfa province. After the determination of the protein content, the venom sample was subjected to enzymatic activity assays to assess phospholipase A2, protease, ʟ-amino acid oxidase, hyaluronidase, 5′-nucleotidase and, phosphodiesterase activities by a spectrophotometry-based method. Protease activity was also assessed by gelatin zymography. Additionally, the fibrinogenolytic activity of the venom was evaluated using fibrinogen zymography and SDS-PAGE methods. The protein profile was obtained by SDS-PAGE (both reduced and non-reduced) and reversed-phase HPLC methods. According to the results, 11 protein bands between approximately 12-240 kDa were observed on non-reduced SDS-PAGE gel while there were nine bands between 12-140 kDa on the reduced gel. Venom proteins of W. morgani were found predominantly between 25-12 kDa. Proteins were separated into at least 19 major and minor protein groups (peaks) by HPLC analysis. The venom of W. morgani showed all tested enzyme activities at varying levels.