Skip to main content

Transformation of antimicrobial into bradykinin‐potentiating peptides during peptic hydrolysis of bovine haemoglobin: identification, release kinetics and reaction network of peptides

The full text article is not available for purchase.

The publisher only permits individual articles to be downloaded by subscribers.

The precursor cleavage of the antimicrobial peptide α107–136 into the bradykinin‐potentiating peptide α110–125 during peptic hydrolysis of bovine haemoglobin was investigated by reverse phase high‐performance liquid chromatography coupled with tandem mass spectrometry. The optimal conditions for the preparation of α107–136 and α110–125 were found to be low and high degrees of hydrolysis respectively. A total of six peptides were identified as being involved in the cleavage process. Moreover, the reaction network of these peptides was developed according to the sequence alignment and their release kinetics. The affinity of pepsin towards different peptide bonds of bovine haemoglobin was also compared based on data from the release kinetics of peptides. In addition, some potentially bioactive peptides were predicted by means of sequence analysis and secondary structure calculations. Copyright © 2006 Society of Chemical Industry
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: bioactive peptide; enzymatic kinetics; haemoglobin; pepsin; protein hydrolysis; reaction network

Document Type: Research Article

Publication date: 2007-02-01

More about this publication?
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more