Elimination of the Cys558-Cys566 bond in Lys78-plasminogen--effect on activation and fibrin interaction

Plasminogen contains a unique disulphide bond, Cys558-Cys566, responsible for the cyclic nature of the peptide sequence surrounding the activation site at Arg561-Val562. A recombinant [Ser558, Ser566]-Lys78-plasminogen variant was produced in which the two cysteine residues were replaced by serine r...

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Veröffentlicht in:	European journal of biochemistry 1998-01, Vol.251 (1-2), p.472-479
Hauptverfasser:	Linde, V, Nielsen, L S, Foster, D C, Petersen, L C
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cricetinae Cysteine - chemistry Disulfides - chemistry Electrophoresis, Polyacrylamide Gel - methods Enzyme Activation Fibrin - metabolism Fibrinolysin - metabolism Lysine Plasminogen - chemistry Plasminogen - drug effects Plasminogen - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Serine Serine Endopeptidases - metabolism Serine Endopeptidases - pharmacology Streptokinase - metabolism Streptokinase - pharmacology Tissue Plasminogen Activator - metabolism Tissue Plasminogen Activator - pharmacology Urokinase-Type Plasminogen Activator - metabolism Urokinase-Type Plasminogen Activator - pharmacology
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