A strong fibrinolytic activity was demonstrated in the vegetable cheese Natto, which is a typical soybean food eaten in Japan. The average activity was calculated at about 40 CU (plasmin units)/g wet weight. This novel fibrinolytic enzyme, named nattokinase, was easily extracted with saline. The mol. wt and pI were about 20,000 and 8.6, respectively. Nattokinase not only digested fibrin but also the plasmin substrate H-D-Val-Leu-Lys-pNA (S-2251), which was more sensitive to the enzyme than other substrates tried. Diisopropyl fluorophosphate and 2,2,2-trichloro-1-hydroxyethyl-o,o-dimethylphosphate strongly inhibited this fibrinolytic enzyme.
In the previous paper,1} wereported on the formation of 2,3-butanediol stereoisomers (R and meso) in Bacillus polymyxa through the action of two kinds ofenzymes. One was a previously known enzyme, /^-butanediol dehydrogenase (EC 1.1.1.4), which catalyzes the reversible reduction of acetoin to butanediol, and the other was a
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