Expression in Escherichia coli of biologically active enzyme by a DNA sequence coding for the human plasminogen activator urokinase.
AUTOR(ES)
Ratzkin, B
RESUMO
We have isolated clones of Escherichia coli strain K-12 that contain a hybrid pBR322 plasmid having a 4.2-kilobase insert of a DNA transcript of the mRNA of human plasminogen activator, urokinase. The bacterially produced enzyme has properties similar to those of urokinase from human fetal kidney cells. Both enzymes occur in discrete forms ranging from 32,000 to 150,000 daltons in size. They react with antibody to purified urokinase from human kidney cells, bind to a benzamidine-Sepharose column, and induce plasminogen-dependent lysis of a fibrin clot.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319558Documentos Relacionados
- Expression of Active Human Tissue-Type Plasminogen Activator in Escherichia coli
- Isolation from human plasma of a plasminogen activator identical to urinary high molecular weight urokinase.
- Secretion of Active Recombinant Human Tissue Plasminogen Activator Derivatives in Escherichia coli
- Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor.
- Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor.
