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It has been found that heparin (Hp) forms a complex with fibrin stabilizing factor (FSF) in vitro. The formation of complex FSF-Hp has been testified by electrophoresis, analytical ultracentrifugation, spectral analysis in the regions of ultra-violet and ultra-red absorption and by study of differential spectrum of complex FSF-Hp. Maximum of specific biochemical activity of the complex FSF-Hp was estabilished when the weight relation between Hp and FSF reached 1:4, at pH 7,3. Complex FSF-Hp diminished specific activity when its formation was carried out in the conditions of raising or reducing weight ratio of Hp. The activity totally disappeared when ratio Hp:FSF was reached 1:1 or 1:15. Complex FSF-Hp obtained in optimal conditions acted as an inhibitor of polymerization (aggregation) of fibrin monomer. It also carried out the lysis of non-stabilized fibrin in the presence or absence of E-aminocaproic acid. The mentioned biochemical activity of complex FSF-Hp is very similar to one of complex fibrinogen-heparin, formation of which in vitro and in vivo and physiological significance we investigated before (2,3)

Passaram-se 40 anos desde qie se proclamou a Comuna de Paris. Seguindo o costume, o proletariado francês honrou com comícios e manisfestações a memória dos homens da revolução de 18 de março de 1871.