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 in | Biochimica et biophysica acta Vol. 1079; no. 3; pp. 316 - 320 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
20.09.1991
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0167-4838 0006-3002 1879-2588 |
DOI: | 10.1016/0167-4838(91)90075-B |