Regulation of Trypsin Activity by Peptide Fraction of an Aqueous Extract of Human Placenta used as Wound Healer

De, Debashree and Bhattacharyya, Debasish and Chakraborty, Piyali Datta (2011) Regulation of Trypsin Activity by Peptide Fraction of an Aqueous Extract of Human Placenta used as Wound Healer. Journal Of Cellular Physiology, 226 (8). pp. 2033-2040.

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    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.

    Item Type: Article
    URI: http://www.eprints.iicb.res.in/id/eprint/37
    Subjects: Structural Biology & Bioinformatics
    Divisions: Indian Institute of Chemical Biology
    Depositing User: Mr Shyamal Nath
    Date Deposited: 28 Sep 2011 19:42
    Last Modified: 19 Jan 2012 16:22
    Official URL: http://dx.doi.org/10.1002/jcp.22535
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