Purification and properties of two fibrinolytic enzymes from Fusarium oxysporum N.R.C.1.
The crude fibrinolytic enzyme preparation from Fusarium oxysporum N.R.C.1 was purified into two enzymes by ammonium sulphate precipitation followed by chromatography on Sephadex G-100 and DEAE-cellulose. Both fibrinolytic enzymes were more active on human than on bovine fibrin. The activity of the "major" enzyme component on human fibrin was 72-fold that of the "minor" enzyme component. Both enzymes had the same temperature (37 degrees C) and pH (6.98) optima. The "minor" enzyme component was more stable than the "major" one against heat and pH treatments. Both enzymes were significantly activated with Co2+ and inhibited with EDTA.
Abdel-Fattah
A F
AF
Department of Natural and Microbial Products Chemistry, National Research Centre, Dokki-Cairo, Egypt.
Ismail
A S
AS
Saleh
S A
SA
D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D000818:Animals; D002417:Cattle; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005337:Fibrin / Q000378:metabolism*; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D005670:Fusarium / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D000596:Amino Acids; D004791:Enzyme Inhibitors; D005343:Fibrinolytic Agents; D005656:Fungal Proteins; D005337:Fibrin; D000645:Ammonium Sulfate