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Retinol-binding protein in human serum: conformational changes induced by retinoic acid binding.

Abstract：

:Polyacrylamide gel electrophoresis and isoelectrofocusing followed by immunoblotting technique with an anti-human retinol-binding protein (RBP) serum were used to study holo-RBP and apo-RBP in human plasma. Three observations were made the technique allowed for the first time to directly and quantitatively analyse holo- and apo-RBP. Holo-RBP represented 97.86 +/- 0.78% and apo-RBP 1.94 +/- 0.73% of the total RBP. All-trans-retinoic acid (RA) was found to bind to apo-RBP and to significantly modify the tertiary structure of the protein; this raises the question of RBP involvement in the transport of RA. reconstitution of holo-RBP using apo-RBP from delipidized serum was achieved only after its incubation with natural all-trans-retinoids such as retinol, 3-dehydroretinol and retinoic acid but not with synthetic analogs of retinoic acid (13-cis-retinoic acid, TMMP, 13-cis-TMMP, TTNPB). It appears that RBP has a structure specificity for natural retinoids.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Siegenthaler G,Saurat JH

doi

10.1016/0006-291x(87)91370-2

subject

Has Abstract

pub_date

1987-03-13 00:00:00

pages

418-23

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(87)91370-2

journal_volume

143

pub_type

杂志文章

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