Abstract

ABSTRACTSnake venom hyaluronidases known as “spreading factor” are not extensively studied. Recently, it is argued that beyond its role as a spreading factor, venom hyaluronidase (HYL) deserves to be explored as a possible therapeutic target for inhibiting the systemic distribution of venom/toxins and also for minimizing local tissue destruction. In this context, in the present study, a low-molecular weight HYL has been isolated from Bungarus caeruleus (Indian krait) venom by single step chromatography on HPLC system. The apparent molecular weight determined by SDS-PAGE is 14 ± 2 kDa, as confirmed by zymogen study and LC–MS as well. The enzyme had optimal pH 6 and temperature 37°C. The Michaelis–Menten constant (Km) was found to be 8.48 µg/mL at 37°C. The activity of purified enzyme was completely inhibited by Ba2+ metal ion and N-acetyl imidazole group-specific agents. This work yielded a highly active HYL from B. caeruleus the first one to be isolated. Further studies on its pharmacological actions will be interesting to develop lead molecules for better management of snakebite.

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