Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications

The binding of retinol, retinyl acetate, retinoic acid and ß-carotene to native, esterified and alkylated ß-lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified ß-lactoglobulin in 1 : 1 molar ratios, with apparent dissociation constan...

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Published inBiochimica et biophysica acta Vol. 1079; no. 3; pp. 316 - 320
Main Authors Dufour, Eric, Haertlé, Tomasz
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 20.09.1991
Elsevier
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Abstract The binding of retinol, retinyl acetate, retinoic acid and ß-carotene to native, esterified and alkylated ß-lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified ß-lactoglobulin in 1 : 1 molar ratios, with apparent dissociation constants in the range of 10 −8 M. The maximum tryptophan fluorescence quenching of unmodified ß-lactoglobulin by ß-carotene is observed at the ligand/protein ratio of 1 : 2. Esterification and alkylation of ß-lactoglobulin shift the ratio of ß-carotene/protein to 1 : 1. In all the cases, except for retinoic acid binding to N-ethyllysyl-BLG, the performed chemical modifications of ß-lactoglobulin enhance protein binding affinity. Measured apparent dissociation constants of ß-carotene complexes with native and modified ß-lactoglobulin are an order of magnitude lower from binding constants of other studied retinoids.
AbstractList The binding of retinol, retinyl acetate, retinoic acid and beta-carotene to native, esterified and alkylated beta-lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified beta-lactoglobulin in 1:1 molar ratios, with apparent dissociation constants in the range of 10(-8) M. The maximum tryptophan fluorescence quenching of unmodified beta-lactoglobulin by beta-carotene is observed at the ligand/protein ratio of 1:2. Esterification and alkylation of beta-lactoglobulin shift the ratio of beta-carotene/protein to 1:1. In all the cases, except for retinoic acid binding to N-ethyllysyl-BLG, the performed chemical modifications of beta-lactoglobulin enhance protein binding affinity. Measured apparent dissociation constants of beta-carotene complexes with native and modified beta-lactoglobulin are an order of magnitude lower from binding constants of other studied retinoids.
The binding of retinol, retinyl acetate, retinoic acid and beta -carotene to native, esterified and alkylated beta -lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified beta -lactoglobulin in 1:1 molar ratios, with apparent dissociation constants in the range of 10 super(-8) M. The maximum tryptophan fluorescence quenching of unmodified beta -lactoglobulin by beta -carotene is observed at the ligand/protein ratio of 1:2. Esterification and alkylation of beta -lactoglobulin shift the ratio of beta -carotene/protein to 1:1. In all the cases, except for retinoic acid binding to N-ethyllysyl-BLG, the performed chemical modifications of beta -lactoglobulin enhance protein binding affinity.
The binding of retinol, retinyl acetate, retinoic acid and ß-carotene to native, esterified and alkylated ß-lactoglobulin was followed by quenching of tryptophan fluorescence. Three studied retinoids bind to native or modified ß-lactoglobulin in 1 : 1 molar ratios, with apparent dissociation constants in the range of 10 −8 M. The maximum tryptophan fluorescence quenching of unmodified ß-lactoglobulin by ß-carotene is observed at the ligand/protein ratio of 1 : 2. Esterification and alkylation of ß-lactoglobulin shift the ratio of ß-carotene/protein to 1 : 1. In all the cases, except for retinoic acid binding to N-ethyllysyl-BLG, the performed chemical modifications of ß-lactoglobulin enhance protein binding affinity. Measured apparent dissociation constants of ß-carotene complexes with native and modified ß-lactoglobulin are an order of magnitude lower from binding constants of other studied retinoids.
Author Haertlé, Tomasz
Dufour, Eric
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Issue 3
Keywords Modification
Ligand binding
N-ethyllysyl-BLG
ß-Carotene
Retinoid
ß-Lactoglobulin
MetBLG
BLG
Lactoglobulins
Carotene
Dissociation constant
Retinoids
Carrier protein
Fluorescence spectrometry
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Snippet The binding of retinol, retinyl acetate, retinoic acid and ß-carotene to native, esterified and alkylated ß-lactoglobulin was followed by quenching of...
The binding of retinol, retinyl acetate, retinoic acid and beta-carotene to native, esterified and alkylated beta-lactoglobulin was followed by quenching of...
The binding of retinol, retinyl acetate, retinoic acid and beta -carotene to native, esterified and alkylated beta -lactoglobulin was followed by quenching of...
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SubjectTerms Analytical, structural and metabolic biochemistry
beta -carotene
Binding and carrier proteins
Biological and medical sciences
Carotenoids - metabolism
Fundamental and applied biological sciences. Psychology
Kinetics
Lactoglobulins - metabolism
Life Sciences
Ligand binding
Modification
Protein Binding
Proteins
retinoic acid
Retinoid
Retinoids - metabolism
retinol
retinyl acetate
Spectrometry, Fluorescence
Tretinoin - metabolism
Vitamin A - analogs & derivatives
Vitamin A - metabolism
ß-Carotene
ß-Lactoglobulin
Title Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications
URI https://dx.doi.org/10.1016/0167-4838(91)90075-B
https://www.ncbi.nlm.nih.gov/pubmed/1911856
https://search.proquest.com/docview/16079691
https://search.proquest.com/docview/72109684
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Volume 1079
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