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

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Title Regulation of Trypsin Activity by
Peptide Fraction of an Aqueous
Extract of Human Placenta used
as Wound Healer
 
Creator De, Debashree
Bhattacharyya, Debasish
Chakraborty, Piyali Datta
 
Subject Structural Biology & Bioinformatics
 
Description 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.
 
Date 2011
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/37/1/JOURNAL_OF_CELLULAR_PHYSIOLOGY%2C_Volume_226%2CIssue_8%2C_2033%2D2040_%2C2011[16].pdf
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.
 
Relation http://dx.doi.org/10.1002/jcp.22535
http://www.eprints.iicb.res.in/37/