The fibrinolytic activity of staphylokinase mutants in the fibrin plate assay.
The fibrinolytic activity of the new plasminogen activator, recombinant staphylokinase, was compared to that of streptokinase and tissue-type plasminogen activator in the fibrin plate assay. The pattern of fibrinolysis by staphylokinase on fibrin plates differs from the other plasminogen activators. A number of mutants of staphylokinase with various amino acids in position 26 substituted for methionine in wild-type staphylokinase were compared with respect to their fibrinolytic potencies. Only the mutants with cysteine or leucine in this position have a fibrinolytic activity comparable to wild-type staphylokinase. The results on the fibrinolytic activities in the fibrin plate assay correlate with those of a plasmin generation assay, the latter is, however, less sensitive.
Hauptmann
J
J
Centre for Vascular Biology and Medicine, Friedrich-Schiller-Universität Jena, Germany.
Gührs
K H
KH
Hartmann
M
M
Schlott
B
B
D000362:Agar; D005342:Fibrinolysis / Q000187:drug effects*; D006801:Humans; D016014:Linear Models; D016015:Logistic Models; D008666:Metalloendopeptidases / Q000235:genetics / Q000494:pharmacology*; D008832:Microchemistry / Q000379:methods*; D009154:Mutation; D010960:Plasminogen Activators / Q000235:genetics / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000494:pharmacology; D013300:Streptokinase / Q000494:pharmacology; D010959:Tissue Plasminogen Activator / Q000494:pharmacology
D011994:Recombinant Proteins; D000362:Agar; D013300:Streptokinase; D010960:Plasminogen Activators; D010959:Tissue Plasminogen Activator; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus