Comparison of activity and conformational changes of ficin during denaturation by urea and guanidine hydrochloride
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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Relation |
http://ir.cftri.com/10127/
PB-13-11 |
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Title |
Comparison of activity and conformational changes of ficin during denaturation
by urea and guanidine hydrochloride
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Creator |
Devaraj, K. B.
Ramesh Kumar, Parigi Prakash, V. |
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Subject |
29 Protein Chemistry
06 Trees And Shrubs 05 Enzymes |
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Description |
The activity and conformational changes of ficin (EC 3.4.22.3), a cysteine protease from Ficus carica
have been investigated during the denaturation by urea and guanidine hydrochloride (GuHCl). The
denaturation of ficin was followed by activity measurements, fluorescence and circular dichroism (CD)
spectroscopic studies. The enzyme activity decreased significantly at low concentration of both urea
and GuHCl before unfolding of the enzyme molecule. The enzyme molecule was resistant for unfolding
by urea under neutral conditions even at higher concentrations. However, the protein is susceptible
to unfolding by urea at lower pH and transition follows a cooperative two-state rule with increasing
concentration of urea. On the other hand, ficin molecule loses its complete structure in presence of 4M
GuHCl under neutral conditions. The GuHCl-induced unfolding occurs in a simple two-state cooperative
process. These results indicate the differential structural stability and fragility of active site of the enzyme
towards denaturation by urea and GuHCl.
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Date |
2011
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Language |
en
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Identifier |
http://ir.cftri.com/10127/1/Process_Biochemistry%2C_Volume_46%2C_Issue_2%2C_February_2011%2C_Pages_458-464.pdf
Devaraj, K. B. and Ramesh Kumar, Parigi and Prakash, V. (2011) Comparison of activity and conformational changes of ficin during denaturation by urea and guanidine hydrochloride. Process Biochemistry, 46. pp. 458-464. |
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