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The interaction of bovine holo- and apo- a-lactalbumin with fatty acids was studied using a partition equilibrium technique and fluorescence spectroscopy. Using there techniques, bovine holo- a-lactalbumin wasfound to be unable to bind fatty acids. Gas chromatography analysis also did not reveal and fatty acids bound to bovine a-lactalbumin that had been isolated using non denaturing conditions. The partition equilibrium showed that bovine apo- a-lactalbumin has one binding site for fatty acids, having association constants of 4.6106 and 5.4105 M1 for oleic and palmitic acids, respectively. The binding of bovine apo- alactalbumin studied by fluorescence spectroscopy also showed the existence of a binding site for oleic acid with a binding constant of 3.3106M1, but the binding parameters could not be estimated for palmitic acid due to low fluorescence enhancement. These results demonstrate that the conformational change induced in a-lactalbumin by the removal of calcium enablesthe protein to interact with fatty acids. |
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2楼2012-12-26 09:19:59
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