Abstract

Two peptides, one undecapeptide and one decapeptide, have been synthesized by the solid phase method. Isotachophoresis has been used as an analytical tool to guide the purification of the peptides. This technique gives qualitative as well as quantitative information about the purification progress. Furthermore, the purity and identity of the final product can be established. The method is rapid, reproducible and easy to perform. Since isotachophoresis also can be used for amino acid analysis, it might have a wide use in peptide chemistry. The two peptides, having the primary sequences around the cross-linking site of fibrin, have been tested in vitro as inhibitors of the fibrin cross-linking. Both peptides were essentially inactive.

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