Localization of the binding site of tissue-type plasminogen activator to fibrin.

Functionally active A and B chains were separated from a two-chain form of recombinant tissue-type plasminogen activator after mild reduction and alkylation. The A chain was found to be responsible for the binding to lysine-Sepharose or fibrin and the B chain contained the catalytic activity of tissue-type plasminogen activator. An ...
extensive reduction of two-chain tissue-type plasminogen activator, however, destroyed both the binding and catalytic activities. A thermolytic fragment, Fr. 1, of tissue-type plasminogen activator that contained a growth factor and two kringle segments retained its lysine binding activity. Additional thermolytic cleavages in the kringle-2 segment of Fr. 1 caused a total loss of the binding activity. These results indicated that the binding site of tissue-type plasminogen activator to fibrin was located in the kringle-2 segment.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Chromatography, Gel, Chromatography, High Pressure Liquid, Dithiothreitol, Fibrin, Macromolecular Substances, Molecular Weight, Peptide Fragments, Thermolysin, Tissue Plasminogen Activator
J. Clin. Invest.
Date: Jul. 01, 1986
Download Curated Data For This Publication
3222
Switch View:
  • Interactions 1