Complete refolding of bovine β-lactoglobulin requires disulfide bond formation under strict conditions

Structural changes and allergenic properties of β‐lactoglobulin upon exposure to high‐intensity ultrasound

“…The β–α transition occurs concomitantly with formation of nonnative internal disulfide bonds and a marked increase in random coil structures . For BLG to be refolded into a native conformation, correct formation of disulphide bonds is critical . Nonnative fold is more stable upon formation of intramolecular S‐S bridges in H60 sample and heat‐treated samples were almost irreversibly refolded into a nonnative conformation.…”

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

“… 14 As it is well known that disturbing the 3-dimensional structure of allergens, including lipocalins, results in diminished IgE binding, 29 , 30 , 31 it seems plausible that Western blotting, because of denaturation, underestimates the frequency of IgE reactivity to nCan f 4. As Hattori et al 32 reported the complete refolding of β-lactoglobulin, a lipocalin, was found to require disulfide bond formation under strict conditions. Our findings are compatible with this view, as our analysis showed that immunoaffinity-purified nCan f 4 contains a functional disulfide bridge ( Fig.…”

Spectroscopic and cytotoxic studies of the novel designed palladium(II) complexes: β-Lactoglobulin and K562 as the targets

“…Members of this family including, retinal and odorant binding proteins as well as the major urinary protein, all share the common structural feature of a ␤-barrel calyx, built from eight anti-parallel ␤-sheets, arranged as an ideal site for hydrophobic ligands [12]. BLG interacts strongly with various hydrophobic ligands such as fatty acids [12], hemin [13], ellipticine [14], aromatic hydrocarbons [15], and carcinogenic hydrocarbons [16] and ions [17]. BLG exists in several genetic variants, but variant A and B are predominant.…”