Metadata of CSIR Papers
View Archive Info| Field | Value | |
| Creator |
Yadav, SC
Kumari, NKP Jagannadham, MV |
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| Subject |
Biophysics
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| Description |
The effect of deglycosylation on the physiological and functional organization of milin was studied under different denaturizing conditions. Trifluoromethanesulfonic acid mediated deglycosylation resulted in insoluble milin, which was found to be soluble only in 1.5 M GuHCl with native-like folded structure. Kinetic stability, proteolytic activity, and dimeric association were lost in deglycosylated milin. Urea-induced unfolding revealed two inactive, highly stable equilibrium intermediates at pH 7.0 and pH 2.0. These intermediates were stable between 5.5-6.5 and 5.0-6.0 M total chaotropes (urea + 1.5 M GuHCl) at pH 7.0 and pH 2.0, respectively. GuHCl-induced unfolding was cooperative and noncoincidental with a broad transition range (2.0-5.0 M) at pH 7.0 and pH 2.0. Equilibrium unfolding of deglycosylated milin by urea and GuHCl substantiates the involvement of various inactive monomeric intermediates. This study provides a way to understand the role of glycosylation in the unfolding mechanism, stability, and functional activity of the serine protease milin.
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| Publisher |
SPRINGERNEW YORK233 SPRING ST, NEW YORK, NY 10013 USA
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| Date |
2011-09-20T12:08:53Z
2011-09-20T12:08:53Z 2010 |
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| Type |
Article
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| Identifier |
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
0175-7571 http://hdl.handle.net/123456789/13545 |
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| Language |
English
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