Abstract J Cell Physiol

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

SB - J Cell Physiol 2011 Aug;226(8):2033-40 TA - J Cell Physiol IP - 8 PG - 2033-40 DP - 2011 FAU - De Debashree D FAU - Chakraborty Piyali Datta PD FAU - Bhattacharyya Debasish D AU - De D AU - Chakraborty P AU - Bhattacharyya D Division of Structural Biology and Bioinformatics, Indian Institute of Chemical Biology (CSIR), Jadavpur, Calcutta, India.

AB - 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, sizeexclusion 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.

Copyright © 2010 Wiley-Liss, Inc. IS - 1097-4652 LA - eng PT - Type:Journal Article PT - Type:Research Support, Non-U.S. Gov't PMID - 21520055 0 0 0 0 21658-26-4 EC 3.4.21.4 DA - 2011 04 26 DCOM - 2011 07 26 PL - United States UOF - J Cell Physiol 2011 Aug;226(8):2033-40 21520055