Aktivitas Trombolitik Fraksi Protein 47 kDa Kelenjar Saliva Aedes albopictus

Abstract

Thrombosis is a pathological condition characterized by the formation of blood clots (thrombi) within blood vessels, which can lead to various thrombotic and cardiovascular disorders. The exploration of novel thrombolytic agents is essential, due to the limitations of currently available therapies. One potential source of bioactive compounds is the salivary gland of the hematophagous mosquitos, Aedes (Ae.) albopictus. The 47 kDa protein fraction isolated from the salivary glands of Ae. albopictus is suspected to be a member of the serpin (serine protease) family, which play a role in preventing blood coagulation during mosquitoes’s blood-feeding process. This study aimed to analyze the thrombolytic activity of the 47 kDa protein fraction from the salivary glands of Ae. albopictus. Female mosquitoes were collected an identified, followed by salivary gland isolation, protein extraction, and protein profiling using SDS-PAGE method. The 47 kDa protein fraction was then isolated and purified through electroelution and dialysis before being evaluated for its proteolytic and thrombolytic activities was tested. Proteolytic activity was assessed using Skim Milk Agar (SMA) for the screening method, while thrombolytic activity was examined through a fibrin plate assay. The final concentration of the 47 kDa protein fraction was 1,33 µg/µl. Results from the proteolytic activity assay showed no clear zone formation of, indicating the absence of proteolytic activity. These results suggest that the 47 kDa protein fraction does not possess direct proteolytic and thrombolytic properties. Instead, the protein may exert its biological role through the inhibition of blood coagulation factors rather than through direct degradation of protein substrates.