Comparison of the Primary Structure of the N-Terminal CNBr Fragments of Human, Bovine and Porcine Plasminogen

Publisher Website
Google Scholar
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 3 highly homologous and 2 variable regions. The heptapeptide sequence responsible for intramolecular interaction is preserved in a conservative region; 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; only 11 exchanges occur between the 2 fragments of animal origin.