Comparison of the primary structure of the N-terminal CNBr fragments of human, bovine and porcine plasminogen.

Abstract

The primary structures of the N-terminal CNBr fragment of human, bovine and porcine plasminogen were determined by automated Edman degradation in a combination of liquid and solid-phase techniques and also by applying the carboxypeptidase method. The comparison of the fragments showed three highly homologous and two variable regions. The heptapeptide sequence responsible for intramolecular interaction is preserved in a conservative region, whereas the sequence of the acidic loop varies considerably between the species. In the bovine and porcine fragments 18 of the 57 residues are exchanged when compared with the fragment of human plasminogen, whereas only 11 exchanges occur between the two fragments of animal origin.