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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Purification of human tissue plasminogen activator with Erythrina trypsin inhibitor.

Seeds of the legume Erythrina latissima contain a 20,000-dalton, single-chain protein that has been shown to inhibit the amidolytic activity of trypsin and tissue plasminogen activator. It had no comparable effect on urokinase. IC50 values of 1.1 X 10(-7) M for tissue plasminogen activator and 6.9 X 10(-10) M for trypsin were determined by titration. When coupled to agarose, the Erythrina inhibitor provided an effective reagent for affinity purification of tissue plasminogen activator from melanoma cell-conditioned tissue culture medium. Using this as a single-step procedure, 270-fold purified enzyme was reproducibly obtained with yields of 90% or greater. Both one- and two-chain forms of tissue plasminogen activator were purified. The enzyme migrated, in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, as a predominant 72,000-dalton doublet with lesser amounts of immunochemically similar, 115,000- and 68,000-dalton components.[1]


  1. Purification of human tissue plasminogen activator with Erythrina trypsin inhibitor. Heussen, C., Joubert, F., Dowdle, E.B. J. Biol. Chem. (1984) [Pubmed]
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