Interaction of human α-lactalbumin with fatty acids:: Determination of binding parameters

被引：12

作者：

Barbana, C. ^{[1
]}

Perez, M. D. ^{[1
]}

Pocovi, C. ^{[1
]}

Sanchez, L. ^{[1
]}

Wehbi, Z. ^{[1
]}

机构：

[1] Univ Zaragoza, Fac Vet, E-50013 Zaragoza, Spain

来源：

BIOCHEMISTRY-MOSCOW | 2008年 / 73卷 / 06期

关键词：

human alpha-lactalbumin; fatty acids; binding; partition equilibrium;

D O I：

10.1134/S0006297908060126

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

收藏

页码：711 / 716

页数：6

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