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Dissociation, aggregation and denaturation of sesame-L -globulin in urea and guanidine hydrochloride solutions.

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Title Dissociation, aggregation and denaturation of sesame-L -globulin in urea and guanidine hydrochloride solutions.
 
Creator Prakash, V.
Nandi, P. K.
 
Subject 03 Proteins
01 Oilseeds
 
Description The effect of urea and GuHCl on the major protein of sesame seed (Sesamum
indicum L.), a-globulin, has been investigated by turbidity, sedimentation
velocity, viscosity, difference spectra and fluorescence spectral measurements.
The protein undergoes dissociation, aggregation and denaturation in the presence
of the above denaturants. There is a critical concentration of the denaturant
where aggregation is maximum. Both denaturation and aggregation are lower in
buffers of high ionic strength. Dissociation and aggregation have been explained
by considering two types of subunits present in the protein mOlecule, one
leading to smaller sedimenting component and the other producing the aggregate.
The amino acid analysis shows that the aggregated fraction is rich in aliphatic
amino acid residues. The endothermic nature of the aggregation process has been
considered to arise from hydrophobic interaction of aliphatic side chains of the
relevant subunits. The protein exists in a more denatured state in CuRCI than in
urea solution.
 
Date 1977
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/3799/1/International%20Journal%20of%20Peptide%20and%20Protein%20Research%2C%20Volume-9%28%20%281977%29%2097-106.pdf
Prakash, V. and Nandi, P. K. (1977) Dissociation, aggregation and denaturation of sesame-L -globulin in urea and guanidine hydrochloride solutions. International Journal of Peptide and Protein Research, 9. pp. 97-106.