The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

Papiz, Miroslav Z.; Sawyer, Lindsay; Eliopoulos, Elias; North, A. C. T.; Findlay, John B. C.; Sivaprasadarao, Asipu; Jones, T. Alwyn; Newcomer, Marcia E.; Kraulis, P.

doi:10.1038/324383a0

Cited by 907 publications

(653 citation statements)

References 31 publications

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“…standing of how the family has evolved, suggesting that it is very much older and more widespread than has been supposed. In contrast with their low conservation at the sequence level, analysis of available lipocalin crystal structures, which include plasma retinol-binding protein (RBP) [11], β-lactoglobulin (Blg) [12], insecticyanin [13], bilin-binding protein (BBP) [14,15], major urinary protein (MUP) and α #u -globulin [16], odorant-binding protein (OBP) [17] and epididymal retinoic acid-binding protein [18], shows that the overall folding pattern common to the lipocalins is highly conserved. The nature of this common structure is now well described (see Figures 1 and 2) [2,11].…”

Section: Subunit Molecularmentioning

confidence: 99%

“…There is increasing evidence, from a wide variety of different tissues, that RBP binding to its target cells occurs via specific surface receptors [27,28]. A cell-surface receptor for α " -microglobulin (A1M) has also been identified [29,30], and there is additional evidence to suggest the existence of receptors for MUP [16], Blg [12,31], and OBP [32]. Epidydimal secretory protein has been shown to bind to the plasma membrane of spermatozoa [33], and may be another lipocalin to act via a specific surface receptor.…”

Section: Receptor Bindingmentioning

confidence: 99%

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The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,513

1,278

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The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level ; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel β-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily : the calycins. Members of the lipocalin family are characterized by several common molecular-

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Section: Subunit Molecularmentioning

confidence: 99%

Section: Receptor Bindingmentioning

confidence: 99%

The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,513

1,278

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“…Sa structure tridimensionnelle a été déterminée récemment par Sawyer et al (1985) et Papiz et al (1986).…”

Section: Introductionunclassified

Traitements de dénaturation appliqués à la β-lactoglobuline avant hydrolyse trypsique

Lung¹,

Pâquet²,

Linden³

1991

Lait

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(Reçu le 10 août 1989; accepté le 11 février 1991) Résumé -La 13-lactoglobuline est isolée en 2 étapes à partir de lactosérum acide par chromatographie d'échange d'ions en «batch» (DEAE-Sephacel) suivie de chromatographie de filtration sur gel (Sephadex G-100).On réalise soit un traitement thermique à 90 oC en milieu acide dilué, soit une coupure des ponts disulfures en milieu dénaturant. La solubilité au pHi est de 99,5% pour la 13-lactoglobuline native, 38% pour le substrat chauffé en milieu acide et 5% pour la 13-lactoglobuline réduite. Ces différents substrats sont alors soumis à un traitement enzymatique par la trypsine à 37 oC et pH 7,5. Les produits obtenus sont caractérisés par la mesure des liaisons peptidiques rompues (méthode au TNBS) et analyse électrophorétique en milieu dissociant (évaluation du poids moléculaire).L'hydrolyse trypsique du substrat dans l'état natif conduit à l'apparition de peptides de petites tailles.Le chauffage en milieu acide dilué modifie le substrat de départ et de nombreux polypeptides apparaissent; la trypsine hydrolyse très rapidement ces produits. La coupure des ponts disulfures induit une hydrolyse de la 13-lactoglobuline par la trypsine en peptides de taille importante qui sont à leur tour hydrolysés.Ces observations viennent souligner "importance des pré-traitements appliqués à un substrat et "intérêt que peut présenter la combinaison de traitements enzymatiques, thermiques et chimiques.

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“…Its structure was determined by Papiz et al [18] by standard crystallographic techniques, showing a similarity to the retinol binding protein. A possible binding site for retinol was identified by model-building.…”

Section: Introductionmentioning

confidence: 99%

Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

Reiners

Nicklaus

Guichard

2000

Lait

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-Interactions between β-lactoglobulin and flavour compounds were analysed by instrumental and sensory studies. Affinity chromatography was used to determine binding constants of flavour substances belonging to different chemical classes. A systematic study on esters, pyrazines and phenolic compounds revealed that the increase in the hydrophobic chain length increases the affinity for the protein. Concerning the 4 diastereoisomers of 3-oxo-p-menthane-8-thiol, only the cistrans isomery led to different binding constants. In general, binding constants increased with increasing log P values, except for the terpenic compounds studied, for which another explanation has to be found, taking into account the geometry of the molecule. Sensory analyses applying a matching test showed that the addition of β-lactoglobulin had no effect on the odour perception of vanillin, but brought about a significant decrease in the odour perception of eugenol.

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The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

Cited by 907 publications

References 31 publications

The lipocalin protein family: structure and function

The lipocalin protein family: structure and function

Traitements de dénaturation appliqués à la β-lactoglobuline avant hydrolyse trypsique

Interactions between ?-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol

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