… of Ca 2+ -depleted bovine α-lactalbumin (apo-α-LA) have been … of apo-α-LA, at pH 2.0, and
an all-or-none transition of apo-α-… secondary and tertiary structure of α-LA were outlined after …

… α-Lactalbumin is the second major protein in bovine milk (2-5% of the total protein in bovine
milk). The human variant has several physiologic functions in the neonatal period. In the …

… camel a-la than in its bovine counterpart. Overall the results … bovine protein in both holo and
apo states. Also CD experiments showed similar secondary structure for camel and bovine a-…

In the presence of 0.5 M NaCl at pH 7.1, the Ca 2+ -free apo form of recombinant bovine α-lactalbumin
(BLA) is sufficiently stabilised in its native state to give well-resolved NMR spectra …

The thermal denaturation of bovine and human apo‐α‐lactalbumins at neutral pH has been
studied by intrinsic protein fluorescence, circular dichroism (CD), and differential scanning …

To better understand the formation mechanism of apo-α-lactalbumin (α-LA)/Oleic acid (OA)
complexes, this research used fluorescence spectroscopy and circular dichroism …

… lysozyme and a-lactalbumin, it may be preferable to use apoa-lactalbumin. In this …
bovine apo-a-lactalbumin is described and the results are compared with those of holoa-lactalbumin…

High affinity binding of Ca 2+ to α-lactalbumin (LA) stabilizes the native structure and is
required for the efficient generation of native protein with correct disulfide bonds from the …

… bovine α -lactalbumin that had been isolated using non denaturing conditions. The partition
equilibrium showed that bovine apo- α -lactalbumin … of bovine apo- α -lactalbumin studied by …

… In the present study, the effect of pressure on the structure of holoand apo-LA was investigated
by fluorescence spectroscopy: the intrinsic fluorescence spectrum and the fluorescence …