Fibrinolysis with a new microplasmin purified of human plasm | 17595
International Research Journals

International Research Journal of Biochemistry and Bioinformatics

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Fibrinolysis with a new microplasmin purified of human plasma


Agustín N. Joison, Gustavo Baiardi, Rocío Donalisio and Federico Gallo

Thrombosis, disease characterized to formation of blood clots, is a cause of death frequently associated with myocardial infarction (IAM), stroke, deep-vein thrombosis, and pulmonary embolism. Microplasmin is a low-molecular-weight protein termed with a molecular weight (Mr) of 28 KDa obtained by Plasmin autolysis process in an alkaline solution. Microplasmin was prepared from pooled human plasma by acetic acid precipitation (pH 6.1) in buffer sodium borate (pH 8.0). Microplasmin was purified with affinity and anionic interchange chromatography. A protein peak with most of the fibrinolytic activity of microplasmin adsorbed in the lysine-Sepharose column and eluted after washing the column with 200 mM of �?Ž�?µ-aminocaproic acid. The second peak eluted with 150 mM with fibrinolytic activity was pooled to gel electrophoresis analysis. Protein named microplasmin with two chains was insolated of human plasma showed fibrinolysis in vitro clot respect control.

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