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Binding of Ca(II), Mg(II), and Zn(II) by 7S fraction of soybean proteins.

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Title Binding of Ca(II), Mg(II), and Zn(II) by 7S fraction of soybean proteins.
 
Creator Rao, A. G. A.
Rao, M. S. N.
 
Subject 03 Proteins
05 Soya bean
 
Description Binding of Ca(ll) or Mg(II) by 7s protein at pH 7.8 appears to occur at the imidazole groups of the
histidine residues of the protein molecule. Zn(II) binding at pH 6.5 also occurs at imidazole groups.
The 78 protein binds more Ca(ll) or Mg(II) in borate buffer than in Tris·HCI buffer of the same pH.
Rate of proteolysis, fluorescence, optical rotatory dispersion, and circular dichroism measurements do
not indicate any conformational change in the protein due to metal ion binding. Ca(Il), Mg(Il), or Zn(II)
increases the heat coagulation of 7s protein. At room temperature the protein is precipitated to an
extent of 40% by Ca(ll), 10% by Mg(lI), and 90% by Zn(II). NaCI (0.5 M) suppresses precipitation
by Ca(ll) or Mg(II) and decreases only slightly precipitation by Zn(ll).
 
Date 1976
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
Rights —
 
Identifier http://ir.cftri.com/3154/1/Journal%20of%20Agricultural%20and%20Food%20Chemistry%2C%20Volume-24%283%20%281976%29%20490-494.pdf
Rao, A. G. A. and Rao, M. S. N. (1976) Binding of Ca(II), Mg(II), and Zn(II) by 7S fraction of soybean proteins. Journal of Agricultural and Food Chemistry, 24 (3). 490-494, 14 ref..