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Abstract: <br /> <br /> <br /> Earthworm has been used as a fibrinolytic agent in East Asia for several thousand years. The aim of the research was to partially purify and identify fibrinolytic enzyme of the local earthworm Pheretima sp. The enzyme was isolated from both fresh ear...
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id-itb.:72562017-09-27T15:39:41Z#TITLE_ALTERNATIVE# Hardiany (NIM 205 03 013), Any Indonesia Theses INSTITUT TEKNOLOGI BANDUNG https://digilib.itb.ac.id/gdl/view/7256 Abstract: <br /> <br /> <br /> Earthworm has been used as a fibrinolytic agent in East Asia for several thousand years. The aim of the research was to partially purify and identify fibrinolytic enzyme of the local earthworm Pheretima sp. The enzyme was isolated from both fresh earthworms and earthworm powder, and then followed by fractionation of 40percent saturated ammonium sulfate salt. The ammonium sulfate fraction was further purified using a Sephacryl S300HR column. Proteolytic activity of the enzyme was determined by the azocasein method, and fibrinolytic activity was determined by its ability to degrade fibrin clots. The crude protein extract and the gel fraction were analyzed by sodium dedocyl sulfate-polyacrylamide gel electrophoresis, and a protein band having protease activity was identified by the zymography method. The clear zone on zymogram showed a protease band of both crude extract and gel fraction. The specific ativity of the gel fraction showed 5 fold higher than that of the crude extract. text |
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Abstract: <br />
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Earthworm has been used as a fibrinolytic agent in East Asia for several thousand years. The aim of the research was to partially purify and identify fibrinolytic enzyme of the local earthworm Pheretima sp. The enzyme was isolated from both fresh earthworms and earthworm powder, and then followed by fractionation of 40percent saturated ammonium sulfate salt. The ammonium sulfate fraction was further purified using a Sephacryl S300HR column. Proteolytic activity of the enzyme was determined by the azocasein method, and fibrinolytic activity was determined by its ability to degrade fibrin clots. The crude protein extract and the gel fraction were analyzed by sodium dedocyl sulfate-polyacrylamide gel electrophoresis, and a protein band having protease activity was identified by the zymography method. The clear zone on zymogram showed a protease band of both crude extract and gel fraction. The specific ativity of the gel fraction showed 5 fold higher than that of the crude extract. |
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Hardiany (NIM 205 03 013), Any |
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