Effect of pH on poppy seed 10S protein.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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| Relation |
http://ir.cftri.com/3966/
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| Title |
Effect of pH on poppy seed 10S protein.
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| Creator |
Srinivas, H.
Narasinga Rao, M. S. |
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| Subject |
03 Proteins
01 Oilseeds |
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| Description |
The effect of acid pH on the 10s protein of poppy seed has been studied by
ultracentrifugation, polyacrylamide gel electrophoresis, turbidity, and difference,
fluorescence and circular dichroism spectra. The protein dissociated into lower
molecular weight fractions in the pH range of 4.0 down to 2.5 judged by ultracentrifugation,
electrophoresis and turbidity measurements. U.V. difference
spectra and fluorescence measurements suggested denaturation of the protein.
Thus, both dissociation and denaturation occurred down to pH 2 . 5 . At more
acid pH values (pH 1.3), reassociation and refolding probably occurred. Circular
dichroism studies showed a large increase in the amplitude of the peak at pH
values of 2.8 and 1.3 indicating that unordered structures are formed at acid pH
values.
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| Date |
1987
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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/3966/1/Int.%20J.%20Peptide%20Protein%20Res.%2029%2C%201987%2C%2084-89.pdf
Srinivas, H. and Narasinga Rao, M. S. (1987) Effect of pH on poppy seed 10S protein. International Journal of Peptide and Protein Research, 29. pp. 84-89. |
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