Kishore Kumar Murthy, N. V. and Narasinga Rao, M. S. (1984) Acid denaturation of mustard 12S protein. International Journal of Peptide and Protein Research (23). pp. 94-103.
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Abstract
The effect of low pH on the molecular properties of mustard 12s protein has
been studied by the techniques of ultracentrifugation, viscometry, electrophoresis,
turbidimetry, U.V. difference spectroscopy, fluorescence spectroscopy
and circular dichroism. Ultracentrifugation and electrophoresis experiments
indicated dissociation of the protein in the pH range 5.0 to 3.0 and below this
pH reaggregation was indicated. Viscosity, turbidimetry, U.V. difference spectroscopy,
fluorescence spectroscopy and circular dichroism studies showed that
denaturation of the protein occurred between pH 5.0 and 3.0 and refolding at
pH values below 3.0.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | acid denaturation; mustard 12s protein |
| Subjects: | 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins 600 Technology > 08 Food technology > 19 Lipids-oils/fats > 04 Mustard seed |
| Divisions: | Protein Chemistry and Technology |
| Depositing User: | Food Sci. & Technol. Information Services |
| Date Deposited: | 19 Mar 2018 05:49 |
| Last Modified: | 19 Mar 2018 05:49 |
| URI: | http://ir.cftri.res.in/id/eprint/2642 |
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