ICAR Research Data Repository for Knowledge Management
Effect of succinylation on the oligometric structure of glycinin.
IR@CSIR-CFTRI
View Archive Info| Field | Value | |
| Relation |
http://ir.cftri.com/4021/
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| Title |
Effect of succinylation on the oligometric structure of glycinin.
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| Creator |
Appu Rao, A. G.
Narasinga Rao, M. S. |
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| Subject |
03 Proteins
05 Soya bean |
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| Description |
By varying the ratio of succinic anhydride to the protein, glycinin, one of the major fractions of soybean proteins, is succinylated to various levels. Sedimentation velocity experiments indicate the dissociation of the protein due to succinylation. Viscosity increases and a blue shIft occurs in the absorption specrrnm. The rate of proteolysis increases. Both dissociation and denaturation of the protein appear to occur. The effect of succinylation on glycinin and arachin, the major protein ofgroundnuts, appears to be different. |
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| Date |
1979
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Language |
en
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| Rights |
—
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| Identifier |
http://ir.cftri.com/4021/1/International%20Journal%20of%20Peptide%20and%20Protein%20Research%2C%20Volume-14%28%20%281979%29%20307-312.pdf
Appu Rao, A. G. and Narasinga Rao, M. S. (1979) Effect of succinylation on the oligometric structure of glycinin. International Journal of Peptide and Protein Research, 14. pp. 307-312. |
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