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RESULTS Biophysical characterization of the rSBA The biophysical characteristics of the rSBA are very much similar to that of the native SBA obtained from the seeds of Glycine max
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By a combined effort of thermal and chaotrope-induced denaturation we have been able to show the profound effect of glycosylation in the confomiational stability and oligomerization of the protein
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The instrument was periodically calibrated with (+) 10-camphorsulphonic acid
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with T^sub m^ close to 330 K (Fig
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This different behavior in the thermograms among the members of a protein family is not new, and it has been reported, for instance, in the thermodynamic unfolding of dimeric histone-like proteins (53)
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J Appl Physiol 2004; 97:1535-1542(49) Agusti AG, Sauleda J, Miralles C, et al
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t] is the random error term
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