[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Acid denaturation of mustard 12S protein.

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.

[img] PDF
Int . J. Peptide Protein Rex. 23, 1984,94-103.pdf - Published Version
Restricted to Registered users only

Download (726kB) | Request a copy

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.com/id/eprint/2642

Actions (login required)

View Item View Item