http://www.cnr.it/ontology/cnr/individuo/prodotto/ID246265
Bovine beta-lactoglobulin: Interaction studies with palmitic acid (Articolo in rivista)
- Type
- Label
- Bovine beta-lactoglobulin: Interaction studies with palmitic acid (Articolo in rivista) (literal)
- Anno
- 2000-01-01T00:00:00+01:00 (literal)
- Alternative label
Ragona, L and Fogolari, F and Zetta, L and Perez, DM and Puyol, P and De Kruif, K and Lohr, F and Ruterjans, H and Molinari, H (2000)
Bovine beta-lactoglobulin: Interaction studies with palmitic acid
in Protein science (Print)
(literal)
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- Ragona, L and Fogolari, F and Zetta, L and Perez, DM and Puyol, P and De Kruif, K and Lohr, F and Ruterjans, H and Molinari, H (literal)
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- Rivista
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- ISI Web of Science (WOS) (literal)
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- Molinari, H (Reprint Author), Univ Verona, Dipartimento Sci & Tecnol, Str Le Grazie, I-37134 Verona, Italy. Univ Verona, Dipartimento Sci & Tecnol, I-37134 Verona, Italy. ICM, Lab NMR, I-20131 Milan, Italy. Fac Vet Zaragoza, Zaragoza 50013, Spain. Netherlands Inst Dairy Res, Dept Biophys Chem & Technol, NL-6710 BA Ede, Netherlands. Univ Frankfurt, Inst Biophys Chem, D-60439 Frankfurt, Germany. (literal)
- Titolo
- Bovine beta-lactoglobulin: Interaction studies with palmitic acid (literal)
- Abstract
- Bovine beta-lactoglobulin (BLG) in vivo has been found complexed with fatty acids, especially palmitic and oleic acid. To elucidate the still unknown structure-function relationship in this protein, the interactions between C-13 enriched palmitic acid (PA) and BLG were investigated by means of one-, two-, and three-dimensional NMR spectroscopy in the pH range 8.4-2.1. The NMR spectra revealed that at neutral pH the ligand is bound within the central cavity of BLG, with the methyl end deeply buried within the protein. The analysis of C-13 spectra of the hole protein revealed the presence of conformational variability of bound PA carboxyl end in the pH range 8.4-5.9, related to the Tanford transition. The release of PA starts at pH lower than 6.0, and it is nearly complete at acidic pH. This finding is relevant in relation to the widely reported hypothesis that this protein can act as a transporter through the acidic gastric tract. Ligand binding and release is shown to be completely reversible over the entire pH range examined, differently from other fatty acid binding proteins whose behavior is analyzed throughout the paper. The mode of interaction of BLG is compatible with the proposed function of facilitating the digestion of milk fat during the neonatal period of calves. (literal)
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