Acid denaturation of mustard 12S protein.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
View Archive Info| Field | Value | |
| Relation |
http://ir.cftri.com/2642/
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| Title |
Acid denaturation of mustard 12S protein.
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| Creator |
Kishore Kumar Murthy, N. V.
Narasinga Rao, M. S. |
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| Subject |
03 Proteins
04 Mustard seed |
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| 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.
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| Date |
1984
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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/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. |
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