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Bovine β-lactoglobulin: Interaction studies with palmitic acid

Published online by Cambridge University Press:  01 July 2000

LAURA RAGONA ,
FEDERICO FOGOLARI ,
LUCIA ZETTA ,
DOLORES M. PÉREZ ,
PILAR PUYOL ,
KEES DE KRUIF ,
FRANK LÖHR ,
HEINZ RÜTERJANS  and
HENRIETTE MOLINARI
LAURA RAGONA
Affiliation:
Laboratorio NMR, ICM, Via Ampère 56, 20131, Milano, Italy
FEDERICO FOGOLARI
Affiliation:
Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, Strada Le Grazie, 37134 Verona, Italy
LUCIA ZETTA
Affiliation:
Laboratorio NMR, ICM, Via Ampère 56, 20131, Milano, Italy
DOLORES M. PÉREZ
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria de Zaragoza, Miguel Servet, 177, 50013 Zaragoza, Spain
PILAR PUYOL
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria de Zaragoza, Miguel Servet, 177, 50013 Zaragoza, Spain
KEES DE KRUIF
Affiliation:
Department of Biophysical Chemistry and Technology, Netherlands Institute for Dairy Research (NIZO), 6710 BA Ede, The Netherlands
FRANK LÖHR
Affiliation:
Institut für Biophysikalische Chemie, University of Frankfurt, Marie-Curie-Str. 9, 60439 Frankfurt, Germany
HEINZ RÜTERJANS
Affiliation:
Institut für Biophysikalische Chemie, University of Frankfurt, Marie-Curie-Str. 9, 60439 Frankfurt, Germany
HENRIETTE MOLINARI
Affiliation:
Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, Strada Le Grazie, 37134 Verona, Italy
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Abstract

Bovine β-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 13C 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 13C spectra of the holo 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.

Keywords

bovine β-lactoglobulinlipocalin binding sitesnuclear magnetic resonancepalmitic acidT1 measurementsTanford transition
Type
Research Article
Information
Protein Science , Volume 9 , Issue 7 , July 2000 , pp. 1347 - 1356
Copyright
2000 The Protein Society

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