Premium
Regulation of trypsin activity by peptide fraction of an aqueous extract of human placenta used as wound healer
Author(s) -
De Debashree,
Chakraborty Piyali Datta,
Bhattacharyya Debasish
Publication year - 2011
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.22535
Subject(s) - trypsin , placenta , peptide , human placenta , aqueous extract , chemistry , fraction (chemistry) , aqueous solution , biochemistry , traditional medicine , pregnancy , fetus , biology , medicine , enzyme , chromatography , organic chemistry , genetics
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. J. Cell. Physiol. 226: 2033–2040, 2011. © 2010 Wiley‐Liss, Inc.