Chickpea seed proteins: conformational changes in 10.3S protein during germination.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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http://ir.cftri.com/3445/
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| Title |
Chickpea seed proteins: conformational changes in 10.3S protein during germination.
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| Creator |
Ganesh, Kumar
Venkataraman, L. V. Appu Rao, A. G. |
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| Subject |
03 Proteins
22 Legumes-Pulses |
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| Description |
Changes that occur in the major 10.3S storage protein of chickpea during germination were monitored by viscosity, heat coagulation, alpha-chymotryptic digestion, circular dichroism, and fluorescence spectral measurements. The hydrodynamic method suggested an alteration in the asymmetry, whereas from the CD spectral studies, it was inferred that the limited ordered structure of the 10.3S protein was considerably reduced during germination. The heat coagulation and free -SH group measurements indicated that changes in the quaternary structure occurred possibly through the scission of 1 of the 3 SS bonds present in 10.3S protein. Evidence of conformational changes in 10.3S protein during germination is also provided by the increased susceptibility of 6-day germination-modified (GM) protein to alpha-chymotryptic digestion as compared to 10.3S protein.
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| Date |
1980
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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/3445/1/J.%20Agric.%20Food%20Chem.%201980%2C%2028%2C%20518-524.pdf
Ganesh, Kumar and Venkataraman, L. V. and Appu Rao, A. G. (1980) Chickpea seed proteins: conformational changes in 10.3S protein during germination. Journal of Agricultural and Food Chemistry, 28 (3). 518-524, 29 ref.. |
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