Owusu, Richard (1992) Thermodynamic analysis of the effect of calcium on bovine alpha-lactalbumin conformational stability. Food Chemistry, 44 (3). pp. 189-194. [Journal article]
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ΔG° Values for bovine alpha-lactalbumin (BAL) unfolding in a range of solvents, including simulated milk ultrafiltrate buffer, were determined. The denaturant used was guanidine hydrochloride. In Ca2+-free solvents fluorescence and ultraviolet (UV) difference absorbance unfolding profiles were non-superimposable leading to ΔG° estimates of 15–17 kJ mol−1 and 21–28 kJ mol−1, respectively. Therefore, the unfolding of BAL was consistent with a three-state reaction. The low and high ΔG° estimates may correspond to the loss of BAL 3° and 2° structure, respectively.The presence of excess Ca2+, two BAL unfolding transitions (I and II) were observed with both spectrophotometric techniques. Transition (II) was associated with a ΔG° value of 52 kJ mol− and is probably identical to a two-state BAL unfolding reaction described previously. Transition (I) appears to signify a novel feature of BAL structure.
|Item Type:||Journal article|
|Faculties and Schools:||Faculty of Life and Health Sciences|
Faculty of Life and Health Sciences > School of Biomedical Sciences
|Research Institutes and Groups:||Biomedical Sciences Research Institute|
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
|Deposited By:||Dr Richard Owusu-Apenten|
|Deposited On:||01 Feb 2011 13:24|
|Last Modified:||01 Feb 2011 13:24|
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