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Equilibrium denaturation of buffalo pituitary growth hormone

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Title Equilibrium denaturation of buffalo pituitary growth hormone
 
Creator Maithal, Kapil
Krishnamurty, H G
Muralidhar, K
 
Description 368-374
To understand the structural properties of buffalo
growth hormone (buGH), the equilibrium denaturation using guanidinium chloride (GdmCl
) was carried out and was monitored by ultraviolet absorption spectroscopy,
intrinsic fluorescence spectroscopy, far UV-circular dichroism and
size-exclusion chromatography. The normalized denaturation transition curves
for each of the above methods were not coincident, showing that buGH does not
follow a simple two state folding mechanism. Further, size-exclusion
chromatography also showed the presence of an associated intermediate
during the unfolding of buGH. It was
observed that in buGH, denaturation resulted in an initial disruption of the
tertiary structure, whereas the secondary structure and the degree of
compactness were disrupted at a higher concentration of the denaturant. This
suggests that buGH follows the hierarchical model of protein folding.
 
Date 2012-12-25T18:46:03Z
2012-12-25T18:46:03Z
2001-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15320
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.38(6) [December 2001]