Biochemical and Biophysical Research Communications
Action of Bauhinia bauhinioides synthetic peptides on serine proteinases
Section snippets
Materials and methods
Enzymes, substrates, and peptides. Human plasma kallikrein (HuPK) (EC 3.4.21.34) was purified by a previously described procedure [18]. Porcine pancreatic kallikrein (PoPK) (EC 3.4.21.35), trypsin (EC 3.4.21.4), human thrombin (EC 3.4.21.5), and plasmin (EC 3.4.21.7) were purchased from Sigma Chemical Company. Human neutrophil elastase (EC 3.4.21.37) and porcine pancreatic elastase (PPE) (EC 3.4.21.36) were purchased from Calbiochem. The H-d-Pro-Phe-Arg-AMC, Suc-Ala-Ala-Pro-Val-AMC,
Results and discussion
Previously published results have shown that fluorogenic substrate derived from the BbKI reactive site and hydrolyzed by bovine trypsin or trypsin-like enzymes from insect sources displays resistance to hydrolysis by other serine proteinases [12], [13], [15]. This led us to investigate the reactivity of BbKI-derived synthetic peptides to target and non-target proteinases (Fig. 1A).
The peptides ESPLRINI-NH2 (P2) and RFESPLRINII-NH2 (P4), containing the amino acid Arg at the P1 position of the
Acknowledgements
We would like to gratefully acknowledge the skilled technical assistance given by Lucimeire A. Santana. This work was partially supported by CAPES, CNPq, FAPESP, and SPDM.
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