Streptokinase catalyzes hydrolysis of amide linkages. Forms a 1:1 complex with plasminogen which is then converted to streptokinase-plasmin. Both streptokinase-plasminogen and streptokinase-plasmin complexes can activate plasminogen. As a result of its interaction with human or rabbit plasminogen, streptokinase undergoes specific fragmentation.
Beta-glucuronidases are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates. Human β-glucuronidase is a type of glucuronidase that catalyzes hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides such as heparan sulfate. In human gut β-glucuronidase converts conjugated bilirubin to the unconjugated form for reabsorption.
A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.