Regulation of trypsin activity by peptide fraction of an aqueous extract of human placenta used as wound healer.

Abstract

An aqueous extract of human placenta, used as wound healer, shows stabilization of trypsin against autodigestion as one of the peptides of the extract binds very strongly with the protease. Trypsin retains 40% of activity at constant level between 20 and 26 days in presence of the extract against complete inactivation in its absence. Inhibition of esterolytic activity and inability to react with p-nitrophenyl-p'-guanidinobenzoate, HCl, an active site directed reagent, by trypsin in presence of a peptide fraction of the extract indicated blocking of the catalytic site of the enzyme. Rayleigh scattering, size-exclusion HPLC, fluorescence resonance energy transfer, and surface plasmon resonance show that fibronectin type III-like peptide present in the extract interacts with trypsin. The peptide-trypsin complex is dissociated in presence of high concentration of substrates. Thus, regulation of trypsin activity by the placental extract is evident.

• Authors: Debashree De, Piyali Datta Chakraborty, Debasish Bhattacharyya
• Journal: Journal of cellular physiology (J Cell Physiol) Vol. 226 Issue 8 Pg. 2033-40 (Aug 2011) ISSN: 1097-4652 [Electronic] United States
• PMID: 21520055 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2010 Wiley-Liss, Inc.

Chemical References

• Benzoates
• Fibronectins
• Peptides
• fibronectin type III like peptide, human
• 4-nitrophenyl 4'-guanidinobenzoate
• Trypsin

Topics

• Benzoates (pharmacology)
• Catalytic Domain (drug effects)
• Female
• Fibronectins (analysis)
• Humans
• Peptides (analysis, pharmacology)
• Placenta (chemistry, drug effects)
• Pregnancy
• Trypsin (metabolism)
• Wound Healing (drug effects)