Interaction of human alpha-lactalbumin with fatty acids: determination of binding parameters.

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Barbana C, Perez MD, Pocovi C, Sanchez L, Wehbi Z

Interaction of human alpha-lactalbumin with fatty acids: determination of binding parameters.

Biochemistry (Mosc). 2008 Jun;73(6):711-6.

PubMed ID
18620538 [ View in PubMed
]
Abstract

The interaction of holo- and apo-forms of human alpha-lactalbumin with fatty acids was studied by a partition equilibrium method. Apo-alpha-lactalbumin, obtained by treatment with EDTA, displays one binding site for fatty acids, the association constants for oleic and palmitic acids being 1.9.10(6) and 4.2.10(5) M(-1), respectively. However, holo-alpha-lactalbumin was unable to bind fatty acids as measured by this technique. Likewise, no fatty acids bound to holo-alpha-lactalbumin, isolated using nondenaturing conditions, were detected by gas chromatography. These results demonstrate that the conformational change induced in alpha-lactalbumin by the removal of calcium enables the protein to interact with fatty acids.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Palmitic AcidAlpha-lactalbuminProteinHumans
Unknown
Not AvailableDetails