Denaturation of glycinin by urea and guanidine hydrochloride.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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http://ir.cftri.com/3693/
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| Title |
Denaturation of glycinin by urea and guanidine hydrochloride.
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| Creator |
Suresh Chandra, B. R.
Appu Rao, A. G. Narasinga Rao, M. S. |
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| Subject |
03 Proteins
05 Soya bean |
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| Description |
Denaturation of glycinin by urea and guanidine hydrochloride (GdnHC1) has
been studied at 30' by viscosity and circular dichroism (CD) measurements.
The kinetics of denaturation by 8M urea at 20, 30, 40 and SOo, and by 6M
GdnHCl at 20' have been measured by monitoring the increase in absorbance
at 287nm as a function of time. Viscosity increased with denaturant concentration
and reached maximum value of - 28 mL/g at 6M GdnHCl and 7M
urea, The (negative) molar ellipticity values in the region 250-200 nm decreased
with increase in denaturant concentration. Analysis of viscosity and CD data
indicated that both sets of data fitted the same curve of fd (fraction of protein
denatured) versus denaturant concentration. The kinetic data followed first
order reaction kinetics. These suggest that denaturation of glycinin by urea/
GdnHCl is a two-state process and follows the same pattern as that of globular
proteins.
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| Date |
1986
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| Type |
Article
PeerReviewed |
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| Format |
pdf
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| Language |
en
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| Identifier |
http://ir.cftri.com/3693/1/Int.%20J.%20Peptide%20Protein%20Res.%2027%2C%201986%2C493-500.pdf
Suresh Chandra, B. R. and Appu Rao, A. G. and Narasinga Rao, M. S. (1986) Denaturation of glycinin by urea and guanidine hydrochloride. International Journal of Peptide and Protein Research, 27. pp. 493-500. |
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