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Binding of Zn(II) by the 11S fraction of soybean proteins.

Rao, A. G. A. and Rao, M. S. N. (1976) Binding of Zn(II) by the 11S fraction of soybean proteins. Journal of Agricultural and Food Chemistry, 24 (3). 487-490, 21 ref..

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Abstract

Binding of Zn(II) by the l1S fraction of soybean proteins in 0.2 M acetate buffer of pH 6.5 was determined by equilibrium dialysis. The Scatchard plot of binding data indicated heterogeneity of binding sites. Binding occurs possibly at the imidazole groups of histidine residues. Addition of 0.5 M NaCI to the buffer or prior treatment of the protein with EDTA had no effect on binding. Zn(1I) binding did not change the sedimentation velocity pattern of the protein or its s20w value. It did not affect toe fluorescence spectrum and ORD in the visible range. However, it increased heat coagulation of the protein. At 4 X 10-3M and higher Zn(II) concentrations the protein was quantitatively precipitated. Precipitation at low concentrations of Zn(II) was suppressed by NaCI but was not at higher concentrations.

Item Type: Article
Uncontrolled Keywords: Zn(II), soybean proteins
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Jul 2016 10:28
Last Modified: 14 Jul 2016 10:28
URI: http://ir.cftri.com/id/eprint/3157

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