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The phenomenon of liquefaction of human fibrin clots by broth cultures or culture filtrates of beta hemolytic streptococci was first described by Tillett and Garner in 1933 (1). The complex mechanism of this reaction, thought at first to be a direct fibrinolytic effect of a streptococcal enzyme, has been elucidated in recent years. Milstone (2) demonstrated that a substance present in plasma, termed "lytic factor," is required for dissolution of the clot; and as a result of the work of Christensen (3, 4), confirmed independently by Kaplan (5), it is now known that the "lytic factor" is a proteolytic enzyme normally present in the plasma as an inactive precursor. The role of the active streptococcal substance is that of an activator of the proteinase precursor, converting it into an active enzyme in a manner analogous to the conversion of trypsinogen to trypsin by enterokinase. The active serum proteinase is responsible for digestion of the fibrin clot. In view of the accumulated evidence regarding the nature of streptococcal fibrinolysis, Christensen and MacLeod (6) have proposed the term streptokinase to replace the term fibrinolysin originally applied to the streptococcal component of the system. They have further suggested the name plasminogen for the inactive form of the serum proteinase and plasmin for the active enzyme. This terminology has been adopted in the present report. The activity of streptokinase derived from group A hemolytic streptococci in promoting the lysis of human fibrin clots is in sharp contrast to its minimal effect on clots of other animal species (1, 4, 7, 8). Although the basis for the apparent

the journal of clinical investigation/the journal of clinical investigation

QUANTITATIVE ANTISTREPTOKINASE STUDIES IN PATIENTS INFECTED WITH GROUP A HEMOLYTIC STREPTOCOCCI: A COMPARISON WITH SERUM ANTISTREPTOLYSIN AND GAMMA GLOBULIN LEVELS WITH SPECIAL REFERENCE TO THE OCCURRENCE OF RHEUMATIC FEVER 1