Skip to main content
padlock icon - secure page this page is secure

Structural and Functional Properties of Kunitz Proteinase Inhibitors from Leguminosae: A Mini Review

Buy Article:

$68.00 + tax (Refund Policy)

Seed proteins that inhibit proteinases are classified in families based on amino acid sequence similarity, nature of reactive site and mechanism of action, and are used as tools for investigating proteinases in physiological and pathological events. More recently, the plant Kunitz family of inhibitors with two disulphide bridges was enlarged with members containing variable number of cysteine residues, ranging from no cysteine at all to more than four residues. The characteristic of these proteins, as well the interactions with their target proteinases, are briefly discussed.

No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Chymotrypsin; Kunitz Proteinase Inhibitors; MEROPS; actin; amino acid sequence; cysteine residues; disulphide bridges; kunitz inhibitors; leguminosae; plant inhibitors; primary structure; proteolysis; reactive site; seed proteins; trypsin inhibitors

Document Type: Research Article

Publication date: August 1, 2011

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