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Acid denaturation of mustard 12S protein.

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Title Acid denaturation of mustard 12S protein.
 
Creator Kishore Kumar Murthy, N. V.
Narasinga Rao, M. S.
 
Subject 03 Proteins
04 Mustard seed
 
Description 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.
 
Date 1984
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/2642/1/Int%20.%20J.%20Peptide%20Protein%20Rex.%2023%2C%201984%2C94-103.pdf
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.