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Updated: Jun 19, 2026
Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
Published on: June 2, 2023
BIOCHEMICAL STUDIES ON THE FIBRINOLYTIC ACTIVITY OF HEMOLYTIC STREPTOCOCCI : I. ISOLATION AND CHARACTERIZATION OF
1Biological Division of the Department of Medicine, The Johns Hopkins Medical School, Baltimore.
Abstract:
THE ACTIVE FIBRINOLYTIC PRINCIPLE PRESENT IN CULTURES OF HEMOLYTIC STREPTOCOCCI CAN BE ISOLATED IN STABLE FORM, AND PARTIALLY PURIFIED BY THE FOLLOWING METHODS: 1. Precipitation of culture filtrate with 3 volumes of 95 per cent ethyl alcohol. 2. Adsorption upon polyaluminum hydroxide B of Willstätter (5) followed by elution with M/10 sodium phosphate buffer, pH 7.3. Concentration can be best accomplished by vacuum dialysis (4) of either culture filtrates or preparations obtained by adsorption and elution. The streptococcal fibrinolysin is characterized by the following properties: 1. It may resist heating to 100 degrees C. for 60 minutes; variations in thermal resistance are described. 2. Partially purified preparations give positive tests for protein. Activity is rapidly and completely destroyed by trypsin or papain. 3. The active principle is demonstrable in dissolved fibrin even after 18 hours incubation.
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